A0A384KE26	5VJ8	30284	set1	-	-	127	131	MemMoRF	extracellular	28726410	-	"The extracellular loops are significantly disordered, due to sparse resonance assignments and the lack of restraints for this region of the protein" ... "The membrane-embedded position of the β-barrel agrees with the 1H/2H exchange data, placing the ring of positively charged Lys and Arg side chains at the extracellular membrane surface, and the two bands of aromatic residues near the membrane-water interfaces" ... "Basic Arg and Lys side chains of Ail (yellow sticks) are at the extracellular membrane surface" ... "The emerging data suggest that protein dynamics may be modulated by LPS. This is intriguing, especially in light of the functional importance of the extracellular loops of Ail and the fact that Y. pestis alters the molecular composition of its outer membrane depending on physiological conditions." ... "The membrane composition, however, appears to have a marked effect on protein dynamics, with LPS enhancing conformational order and slowing down the 15N transverse relaxation rate."	nanodisc	-	A-104-108	X-ray structure 3QRA has missing atoms in this region.	-	disorder to disorder	papers	papers
E2FZM5	-	-	-	-	-	-	-	MemMoRF	unknown	26650755	-	"we find that Mtb protein SocB lacks signatures of order and of structural elements when by itself in vitro. It appears to be an intrinsically disordered protein, based on CD, NMR, diffusion, and thermal melting experiments. However, in the presence of a synthetic phospholipid bilayer, SocB appears to become helical." ... "Altogether, these findings suggest that by itself SocB is intrinsically disordered. Interestingly, SocB interacts with a synthetic phospholipid bilayer and becomes helical, which suggests that it may be membrane-associated."	MSP1D1:DPPC nanodisc	-	-	No data available about the exact regions.	-	disorder to order	papers	papers
F1NHE9	3SPC	-	-	-	A	61	69	MemMoRF	intracellular	21874019	-	"On PIP(2) binding, a flexible expansion linker contracts to a compact helical structure"	-	MP	A-26-34	-	A-43-69;A-121-149;B-43-69;B-121-149;C-43-69;C-121-149;D-43-69;D-121-149	disorder to order	papers	papers
O00168	2JO1	16168	set1	-	A	80	90	MemMoRF	intracellular	17511473	-	"A fourth helix (H4), containing the S63 and S68 consensus sites for phosphorylation by PKA and PKC, is separated from H3 by a flexible linker with significantly smaller values of the 1H/15N NOE, and significantly greater peak intensities." ... "Helix H4 associates with the micelle surface, and is buried in the micelle to a similar extent as residues 39 to 45 at the end of the transmembrane segment." ... "Fragment A (residues 1 to 50) includes helices H1 to H3, and fragment B (residues 51 to 72) includes the flexible linker and helix H4."	SDS	SP	A-60-70	-	A-16-36	disorder to order	calculations	calculations, papers, structures
O00499	2RMY	11050	set1	-	A	12	33	MemMoRF	intracellular	18658220	-	"Structure calculation, dynamic measurements, and a fast amide proton exchange confirmed the earlier proposed amphipathic character of the induced helix but also revealed a disordered N-terminal part of the amphipathic helix that is highly flexible and exposed to the solvent." ... "The predicted N-terminal amphipathic helix-0 of the human Bin1/Amphiphysin II BAR domain comprises residues 1–33 (14,45). This part of the molecule is disordered in the absence of lipids and thereby unresolved in the crystal structure (12)." ... "Hence, the micelle environment generally stabilizes the helix, leading to a range of α-helicities of 40 to 50% (SDS1: 48%; SDS3: 50%; DPC: 40%) for residues 12–30 during the final simulated 20 ns."	SDS	-	A-12-33	-	-	disorder to order	PFAM, calculations, papers	calculations, papers
O00499	2RND	11049	set1	-	A	12	33	MemMoRF	intracellular	18658220	-	"Structure calculation, dynamic measurements, and a fast amide proton exchange confirmed the earlier proposed amphipathic character of the induced helix but also revealed a disordered N-terminal part of the amphipathic helix that is highly flexible and exposed to the solvent." ... "The predicted N-terminal amphipathic helix-0 of the human Bin1/Amphiphysin II BAR domain comprises residues 1–33 (14,45). This part of the molecule is disordered in the absence of lipids and thereby unresolved in the crystal structure (12)." ... "Hence, the micelle environment generally stabilizes the helix, leading to a range of α-helicities of 40 to 50% (SDS1: 48%; SDS3: 50%; DPC: 40%) for residues 12–30 during the final simulated 20 ns."	DPC	-	A-12-33	-	-	disorder to order	PFAM, calculations, papers	calculations, papers
O39928	2M6X	19162	set1	-	-	780	786	MemMoRF	intracellular	23739335;20727850;20667830	-	"The cytosolic loop 33–39 at the membrane interface contains the fully conserved dibasic motif shown to be crucial for infectivity in vivo as well as ion channel activity and function of the protein in virus release (7, 10, 11, 15). The conserved hydrophobic nature of segment 36–39 is consistent with its location at the hydrophilic-hydrophobic membrane interface (Figs. 5 and ​and6,6, C and D)."	DPC, monomer	MP	A-33-39;B-33-39;C-33-39;D-33-39;E-33-39;F-33-39	780-786: oligomer: helix, monomer: loop	-	disorder to order	calculations	papers
O75324	1ZZA	6715	set1	-	A	61	79	MemMoRF	intracellular	16246365	-	"The structure is composed of a single transmembrane helix from residues 10–33, a large dynamic unstructured linker region, and a distorted cytoplasmic helix from residues 61–79 that interacts with the surface of the lipid bilayer. The organotin-binding site (Cys32 and Cys34) and the flanking putative 14-3-3ζ binding domain (residues 39–45) are located at the membrane interface and are accessible for binding interactions."	SDS	SP	A-63-81	MemMoRF is in between two disordered regions, only structure for this protein.	A-13-33	disorder to order	calculations	calculations, papers, structures
O75324	1ZZA	6715	set1	-	A	34	45	MemMoRF	intracellular	16246365	-	The organotin-binding site (Cys32 and Cys34) and the flanking putative 14-3-3ζ binding domain (residues 39–45) are located at the membrane interface and are accessible for binding interactions."	SDS	SP	A-63-81	This disordered region is ordered and helical on the surface of SDS micelle.	A-13-33	disorder to order	DisProt	calculations, papers
O88339	1H0A	-	-	-	A	3	15	MemMoRF	intracellular	12353027	-	"We have discovered that formation of an amphipathic alpha-helix in epsin is coupled to PtdIns(4,5)P(2) binding." ... "This helix is orientated such that it has the potential to interact with the membrane." ... "Mutants of residue L6 to E, Q, H and W showed less binding to liposomes, implying a role for helix 0 in membrane interactions" ... "Compared with an earlier structure of this domain solved in the absence of a lipid head group14 (Fig. 2a, middle structure), a new helix became ordered at the N-terminus, which we have named ‘helix zero’."	-	-	A-3-15	-	-	disorder to order	papers	papers
P00533	1Z9I	6579	set1	-	A	676	686	MemMoRF	intracellular	15840573	-	"Our results provided evidence for the binding of JX domain peptide to micelles, causing the formation of three helical domains; from residues Lys652 to Arg662, Asn676 to Glu685, and Phe688 to Leu694. All helices were shown to be amphipathic and to use their hydrophobic sides for micelle surface binding (Fig. 7)." ... "...phosphorylation disrupting the helical structure and/or micelles binding of helix 1, causing the recessive basolateral signal (658LL659) to become accessible and thus strengthen the basolateral signal to dominate over the lysosomal sorting signal."	DPC	SP	-	-	-	disorder to order	calculations, papers	calculations, papers, structures
P00533	1Z9I	6579	set1	-	A	700	709	MemMoRF	intracellular	15840573	-	"Our results provided evidence for the binding of JX domain peptide to micelles, causing the formation of three helical domains; from residues Lys652 to Arg662, Asn676 to Glu685, and Phe688 to Leu694. All helices were shown to be amphipathic and to use their hydrophobic sides for micelle surface binding (Fig. 7)."	DPC	SP	-	-	-	disorder to order	calculations, papers	calculations, papers, structures
P00533	1Z9I	6579	set1	-	A	712	718	MemMoRF	intracellular	15840573	-	"Our results provided evidence for the binding of JX domain peptide to micelles, causing the formation of three helical domains; from residues Lys652 to Arg662, Asn676 to Glu685, and Phe688 to Leu694. All helices were shown to be amphipathic and to use their hydrophobic sides for micelle surface binding (Fig. 7)." ... "The relevance of this structure, in which the JM-A segment is helical, is uncertain because one portion of this peptide is normally integrated into the folded structure of the kinase domain core as a β strand, but instead adopts an α-helical conformation in this micelle-bound peptide."	DPC	SP	A-8-18;A-32-41;A-44-50	-	-	disorder to order	calculations, papers	calculations, papers, structures
P00533	2M20	18888	set1	-	A,B	676	686	MemMoRF	intracellular	23374349	-	"Our NMR analysis shows that the formation of the JM-A helix is coupled to the configuration of the transmembrane helices and occurs outside of the membrane. Molecular dynamics simulations suggest that when EGFR is in an inactive conformation, the LRRLL motif within the JM-A segment is buried in the membrane (Arkhipov et al., 2013), consistent with NMR data for the isolated juxtamembrane segment of EGFR in detergent micelles (Choowongkomon et al., 2005)."	DMPC&DHPC bicelle	SP	A-35-45;B-35-45	-	A-5-27;B-5-27	disorder to order	calculations, papers	calculations, papers, structures
P00533	2N5S	25729	set1	-	A	676	686	MemMoRF	intracellular	26440883	-	"Our data reveal that the chain of EGFR-TMJMA forms two separate helices (TMD and JMA) on residues 646 − 670 and 676 − 686 in DPC micelles."	DPC	SP	A-38-48	-	A-8-30	disorder to order	calculations, papers	calculations, papers, structures
P00533	-	-	-	-	-	676	686	MemMoRF	intracellular	23374350	-	"The JM-A dimer was so constructed that the hydrophobic sides of the amphipathic JM-A helices were in contact with each other. Notably, simulations of this model showed that the JM-A helices were less stable with DMPC lipids than with POPS/POPC lipids." ... "Notably, the JM-A, which was initially placed in solution away from the POPC/POPS membrane, became embedded in the membrane with the JM-A hydrophobic residues buried in the bilayer interior and the basic residues paired with the head groups of the charged lipid." ... "Taken together, these results support a scenario in which the JM-A conformations alternate between the antiparallel JM-A helix dimer and separated JM-A embedded in the membrane, the former corresponding to the active and the latter to the inactive state."	-	SP	-	-	-	disorder to order	calculations, papers	calculations, papers, structures
P00533	-	-	-	-	A	676	686	MemMoRF	intracellular	25779975	-	"Our simulations reveal that models of the TM helix and a short 20 residue JM regions of all 58 known human RTKs are able to induce bilayer reorganizations in the form of clustering of PIP2 and PS lipid molecules into shells around the JM region. Selectivity for certain lipid species was evident, with PIP2 found to have the greatest propensity to cluster around the JM regions of all receptors."	-	SP	-	-	-	disorder to order	calculations, papers	calculations, papers, structures
P01501	6DST	-	-	-	-	44	69	MemMoRF	extracellular	26561987	-	"The C-terminal PLP peptide transitioned from a random coil to an α-helix in the presence of trifluoroethanol." ... "Both melittin and the PLP peptide have basic residues near their C-terminus and can form amphipathic helices that interact with lipid membranes."	TFE	tm	A-1-26	-	-	disorder to order	papers	papers
P01730	2KLU	16853	set1	-	A	428	438	MemMoRF	intracellular	19781520	-	"In summary, the structure of the transmembrane and cytoplasmic domains of CD4 can be described by a very stable and rigid transmembrane α-helix (372–395) and a second cytoplasmic α-helix (403–413), which is reasonably stable even at 45 °C supported by helix-type NOE patterns, H/D exchange experiments, and heteronuclear NOE values. Obviously, the amphipathic character of the helix tethers the structure to the micellar surface. Notably, the region in HIV-1 VpU, which is responsible for CD4 binding, also features a long amphipathic helix [53], [54]."	DPC	SP	A-40-50	-	A-9-30	disorder to order	DisProt, DIBS, MFIB	calculations, papers
P02945	1BHA	-	-	-	A	78	80	MemMoRF	intracellular	8307023	-	"In micelles, the second a helix is terminated by C-cap Gly63, adopting a conformation characteristic of a left-handed helix. Resi- dues Gly65 to Thr67 form the turn of a right-handed helix. In the isotropic medium of the organic mixture, the C-terminal region of residues 65-71 lacks an ordered structure." ... "side-chain conformations in the regions of resi- dues 8-32 (in both milieus), and 42-64 (organic mixture) and 39 -62 (micelles), with well-defined a-helical backbone structure" ... "Thus, in contrast to the isotropic organic mix- ture, the water-detergent interface induces the formation of the helical structure in this cross-linking region, while the relative orientation of this helix toward the next transmem- brane segment is stipulated by the sequence of the protein,"	SDS micelles	MP	A-65-67	-	A-10-29;A-44-62;A-80-96;A-108-127;A-135-154;A-173-191;A-204-223	disorder to order	papers	papers
P02945	1BHB	-	-	-	A	78	80	MemMoRF	intracellular	8307023	-	"In micelles, the second a helix is terminated by C-cap Gly63, adopting a conformation characteristic of a left-handed helix. Resi- dues Gly65 to Thr67 form the turn of a right-handed helix. In the isotropic medium of the organic mixture, the C-terminal region of residues 65-71 lacks an ordered structure." ... "side-chain conformations in the regions of resi- dues 8-32 (in both milieus), and 42-64 (organic mixture) and 39 -62 (micelles), with well-defined a-helical backbone structure" ... "Thus, in contrast to the isotropic organic mix- ture, the water-detergent interface induces the formation of the helical structure in this cross-linking region, while the relative orientation of this helix toward the next transmem- brane segment is stipulated by the sequence of the protein,"	methanol-chloroform	MP	A-65-67	-	A-10-29;A-44-62;A-80-96;A-108-127;A-135-154;A-173-191;A-204-223	disorder to order	papers	papers
P04156	2LBG	17558	set1	-	A	110	136	MemMoRF	intracellular	22128151	-	"The CHR adopts a curved α-helical conformation in the presence of DPC micelles." ... "But after the addition of the first aliquot of DPC, two sets of resonances were observed at a 1:1 ratio where one set corresponded to the α-helical structure of the CHR peptide, and the second to an unknown conformation ..."	DPC	-	A-1-27	-	-	disorder to order	DisProt	papers
P04370-5	2LUG	18520	set1	-	A	83	94	MemMoRF	intracellular	22947219	-	"Upon association with the lysophospholipid micelles, full-length MBP or peptide fragments thereof will undergo partial disorder-to-order transitions.(5, 6, 13, 34)" ... "experimental and theoretical results agreed well with one another, despite the independence of the starting structures and analyses, both showing membrane association via the amphipathic α-helix"	DPC	-	A-11-20	-	-	disorder to order	DisProt, papers	calculations, papers
P04370-5	X	6857	set1	-	-	83	94	MemMoRF	intracellular	19519451	-	"A highly-conserved central domain presents an amphipathic alpha-helix in association with a phospholipid membrane" ... "In our study [99], the chemical shift index analyses indicated an α-helical conformation of a 10- residue segment of the polypeptide (residues V83-T92) when in a membrane-mimetic environment," ... "In an aqueous environment, there was conflicting evidence of secondary structure formation" ... "this segment of MBP would only form a stabilised α-helix in the presence of a membrane or membrane-mimetic environment."	aqueous solution	-	-	-	-	disorder to order	DisProt, papers	calculations, papers
P04370-5	X	6857	set2	-	-	83	94	MemMoRF	intracellular	19519451	-	"A highly-conserved central domain presents an amphipathic alpha-helix in association with a phospholipid membrane" ... "In our study [99], the chemical shift index analyses indicated an α-helical conformation of a 10- residue segment of the polypeptide (residues V83-T92) when in a membrane-mimetic environment," ... "In an aqueous environment, there was conflicting evidence of secondary structure formation" ... "this segment of MBP would only form a stabilised α-helix in the presence of a membrane or membrane-mimetic environment."	organic solution	-	-	-	-	disorder to order	DisProt, papers	calculations, papers
P04370-5	X	6857	set3	-	-	83	94	MemMoRF	intracellular	19519451	-	"A highly-conserved central domain presents an amphipathic alpha-helix in association with a phospholipid membrane" ... "In our study [99], the chemical shift index analyses indicated an α-helical conformation of a 10- residue segment of the polypeptide (residues V83-T92) when in a membrane-mimetic environment," ... "In an aqueous environment, there was conflicting evidence of secondary structure formation" ... "this segment of MBP would only form a stabilised α-helix in the presence of a membrane or membrane-mimetic environment."	DPC	-	-	-	-	disorder to order	DisProt, papers	calculations, papers
P04370-5	-	-	-	-	-	142	154	MemMoRF	intracellular	20831157	-	"MBP is an intrinsically disordered protein that undergoes extensive post-translational modifications" ... "Our results show that on binding to a lipid bilayer, the Y142−L154 segment in rmC1 forms an amphipathic α-helix"	DMPC (in silico)	-	-	-	-	disorder to order	DisProt, papers	calculations, papers
P04370-5	-	-	-	-	-	142	154	MemMoRF	intracellular	28380689	-	"The classic MBP is intrinsically disordered in aqueous solution but has three distinct α‐helical regions that form transiently and are stabilized by membrane association, representing molecular recognition fragments (α‐MoRFS)"	-	-	-	-	-	disorder to order	DisProt, papers	calculations, papers
P04624	1JAU	-	-	-	A	665	683	MemMoRF	extracellular	11583156	-	"The helical structure of gp41W in membrane-mimetic DPC micelles described here confirms the previous suggestion that this sequence forms a helix when interacting with phospholipid bilayers… gp41W inserts perpendicular to the bilayer normal, near the membrane interfacial region"	DPC	SP	A-1-19	-	A-21-41	disorder to order	papers	papers
P04624	1JAV	-	-	-	A	665	683	MemMoRF	extracellular	11583156	-	"The helical structure of gp41W in membrane-mimetic DPC micelles described here confirms the previous suggestion that this sequence forms a helix when interacting with phospholipid bilayers… gp41W inserts perpendicular to the bilayer normal, near the membrane interfacial region"	DPC	SP	A-1-19	-	A-21-41	disorder to order	papers	papers
P04626	2N2A	25593	set1	-	A,B	683	696	MemMoRF	intracellular	26585403	-	"On the first stage, the structure of dimer subunit was calculated, revealing the presence of two α-helical regions, corresponding to TMD (residues 650–678) and JMA (683–696) and connected by a disordered loop. NMR data obtained for HER2-TMJMA in the micellar environment. e show here that JMA regions are membrane bound in DMPC/DHPC bicelles. Works with EGFR reveal that JMA forms only unstable and transient helix in lipid bicelles [19] and HER2 JMA is completely disordered in the presence of anionic bicelles according to our data . all EGFR/HER members have similar distribution of charged/polar and hydrophobic residues in JMA segments (Fig. S11): they contain KRTLRRLL or synonymous motifs and are charged at the C-terminus. Therefore, we can assume that HER kinase may be activated not only by the parallel/antiparallel arrangement of its JMAs but also by the mode of JMA/membrane interaction."	DPC	SP	A-40-53;B-40-53	-	A-10-32;B-10-32	disorder to order	calculations, papers	calculations, papers
P05067	1AML	5400	set1	-	A	685	695	MemMoRF	extracellular	7588758	10.1111/j.1432-1033.1995.293_1.x	"The main secondary- structure elements found by chemical-shift analysis, sequential and medium-range NOESY data, and NOE-based restrained molecular-dynamics calculations were two helices, Gln15 -Asp23 and Ile31- Met35, whereas the rest of the peptide was in random-coil conformation."	aqueous environment	SP	A-14-24	-	A-31-51	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05067	2LFM	17764	set1	-	A	685	695	MemMoRF	extracellular	21726530	-	"Amyloid-beta (1–40) forms a 310 helix from H13 to D23" ... "we have solved the high-resolution structure of Aβ1–40 at 15 °C at pH 7.3 with 50 mM NaCl. Under this condition Aβ1–40 adopts a folded conformation notably different from that seen in most previous NMR experiments" ... "In all structures with organic solvents (TFE or HFIP), the central hydrophobic core (17LVFFA21) of Aβ1–40 and Aβ1–42 forms a helix similar to that observed in our structure [32], suggesting this region is the most favorable for helix formation in the absence of organic cosolvents."	aqueous environment	SP	A-14-24	-	A-31-51	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05067	2LLM	18080	set1	-	A	685	695	MemMoRF	extracellular	22649674	-	"The structure obtained in dodecylphosphocholine micelles consists of two α-helices: a short surface-associated juxtamembrane helix (Lys687-Asp694) and a long transmembrane helix (Gly700-Leu723), both connected via a mobile loop region."	DPC micelle	SP	A-2-12	-	A-19-39	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05067	2LOH	-	-	-	A,B	685	695	MemMoRF	extracellular	22584060	-	"the juxtamembrane region Gln(686)-Val(695) constitutes the nascent helix, also sensing the dimerization."	DPC	SP	A-2-12;B-2-12	-	A-19-39;B-19-39	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05067	2LP1	15775	set1	-	A	685	695	MemMoRF	extracellular	18702528	-	"While the extreme N-terminus of C99 appears to be largely disordered, our data revealed the presence of a short α-helix that extends from residues Phe690 through Glu693 (see Figure 1). Moreover, it was observed that the consecutive Phe residues in this helix are buried in the membrane surface, with the preceding Val and following Ala residues also being partially buried. These results can be compared to corresponding results from studies of the amyloid-β polypeptides under micelle-associated conditions. Studies of the Aβ polypeptides bound to SDS micelles under neutral pH conditions concluded that these polypeptides include an extramembrane helix that starts at Tyr681 or Gln686 and then terminates at Val695 (26, 30), which is of greater length than observed in this study of C99. A second helix in the Aβ polypeptides starts at essentially the same position as for the TMD of C99 (Lys699) and terminates several residues from their C-termini (at Val711 and Ala713 for Aβ42 and Aβ40, respectively). The significant structural difference between LMPG-micellar C99 and the SDS-micellar Aβ polypeptides likely reflects different modes of membrane interactions for these molecules."	LMPG micelle	SP	A-15-25	-	A-32-52	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05067	-	-	-	-	A	685	695	MemMoRF	extracellular	22654059	-	"A short extracellular “N-helix”(residues 688 to 694) is connected by an interfacial “N-loop” (695 to 699) to the helical TMD (700 to 723). The N-helix is embedded in the membrane surface and dynamically samples a range of orientations around the TMD helix axis (Fig. 1B)."	bicelle	SP	A-15-25	-	A-32-52	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05067	2LP1	15775	set1	-	A	761	770	MemMoRF	intracellular	18702528	-	"The third helix is observed at the extreme C-terminus of C99, starting at Thr761 and extending through N770. This latter observation is reminiscent of results from previous NMR studies of the isolated cytosolic domain of C99 under micelle-free conditions showing this segment to have transient helical character (38, 39). It is acknowledged, however, that our studies of C99 were carried out in the presence of a 22-residue C-terminal purification tag, which could promote the formation of this third helix, although it is much more likely that formation of a stable C-terminal helix results from its capacity to form an amphipathic helix that binds with modest avidity to the micelle surface (see below)."	LMPG micelle	SP	A-91-100	-	A-32-52	disorder to order	DIBS	calculations, papers
P05067	-	-	-	-	A	761	770	MemMoRF	intracellular	22654059	-	"A third helix at the C terminus (residues 762 to 770) is surface-associated but is structurally uncoupled from the TMD by the intervening 38-residue “C-loop” (734 to 761)."	bicelle	SP	A-15-25;A-91-100	-	A-32-52	disorder to order	DIBS	calculations, papers
P05067	2MJ1	19701	set1	-	A	685	695	MemMoRF	extracellular	-	-	-	aqueous environment	SP	A-1-11	-	A-15-35	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05106	1S4X	-	-	-	A	770	784	MemMoRF	intracellular	15024114	-	"Immediately next to the loop is the N744PLY747 motif that forms an inverse turn, which is the start point for the second helix" ... "The formation of the C-terminal helix is surprising, because it was absent in the structure of the αIIb/β3 tail complex in aqueous solution. Because no long-range NOEs were observed between the N- and C-terminal helices, the formation of the C-terminal helix is likely induced and stabilized by the docking of the NPLY turn onto DPC."	DPC	SP	A-49-63	-	-	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05106	2KNC	16496	set1	entity2	B	751	766	MemMoRF	intracellular	19805198	-	-	organic solvent	SP	-	-	B-10-32	disorder to order	DisProt, DIBS	calculations, papers
P05106	2KNC	16496	set1	entity2	B	770	784	MemMoRF	intracellular	19805198	-	"At the TM-CT border, the spatial positions of the positively charged groups of αIIb K989/β3 K716 (Fig. 1D) suggest that they begin the cytoplasmic regions. However, it is possible that the side chains following membrane-proximal residues αIIb V990-F993, β3 L717-I721 are inserted into or anchored onto the membrane (Fig. 1D), which may stabilize the relative orientations of the TM helices."	organic solvent	SP	B-42-57;B-61-75	-	B-10-32	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05106	2KV9	16771	set1	-	A	751	766	MemMoRF	intracellular	21156831	-	"As expected, TMproxH was predicted to partition into the bilayer perpendicular to the membrane as an extension of the TM helix, whereas CytoH1 and CytoH2 were predicted to lie along the membrane surface, stabilized by hydrophobic residues Phe727 and Phe730 in CytoH1 and Leu746, Tyr747, Ala750, Phe754, and Ile757 in CytoH2" ... "HDX of the β3 cytoplasmic domain conjugated to lipid." ... "Asn743-Thr762 was not observed in the absence the bilayers [fig4]"	DPC	SP	A-38-53	-	B-6-28	disorder to order	DisProt, DIBS	calculations, papers
P05106	2KV9	16771	set1	-	A	770	784	MemMoRF	intracellular	21156831	-	"As expected, TMproxH was predicted to partition into the bilayer perpendicular to the membrane as an extension of the TM helix, whereas CytoH1 and CytoH2 were predicted to lie along the membrane surface, stabilized by hydrophobic residues Phe727 and Phe730 in CytoH1 and Leu746, Tyr747, Ala750, Phe754, and Ile757 in CytoH2" ... "HDX of the β3 cytoplasmic domain conjugated to lipid." ... "Asn743-Thr762 was not observed in the absence the bilayers [fig4]" ... Results of HDX experiments (Admin): "the intermediate fragment spanning a portion of the loop and all of CytoH2 had four protected amides (Asn743-Thr762); and the most C-terminal fragment (Asn756-Thr762) had only one protected amide. These results confirmed the location of the helices identified by NMR, as well as the hierarchy of increasing disorder that progresses from the N terminus to the C terminus of the β3 cytoplasmic domain."	DPC	SP	A-57-71	-	B-6-28	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05106	2LJD	17930	set1	-	A	751	766	MemMoRF	intracellular	21956114	-	"Moreover, we have demonstrated that several residues of β3NP (Trp739, Thr741, Ala742, Pro745, and Tyr747) could interact with DPC micelles and these interactions initiate the formation of a second short α-helical region (Leu746-Asn756), which is not generally observed in either aqueous β3 or αIIbβ3 heterodimer" ... ". In this study, we also have accumulated the first direct evidence that tyrosine phosphorylation affects the structure and the association of 3CT with membrane."	DPC	SP	A-30-45	-	-	disorder to order	DisProt, DIBS	calculations, papers
P05106	2LJD	17930	set1	-	A	770	784	MemMoRF	intracellular	21956114	-	"Moreover, we have demonstrated that several residues of β3NP (Trp739, Thr741, Ala742, Pro745, and Tyr747) could interact with DPC micelles and these interactions initiate the formation of a second short α-helical region (Leu746-Asn756), which is not generally observed in either aqueous β3 or αIIbβ3 heterodimer" ... ". In this study, we also have accumulated the first direct evidence that tyrosine phosphorylation affects the structure and the association of 3CT with membrane."	DPC	SP	A-49-63	-	-	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05106	2LJE	17931	set1	-	A	751	766	MemMoRF	intracellular	21956114	-	"Moreover, we have demonstrated that several residues of β3NP (Trp739, Thr741, Ala742, Pro745, and Tyr747) could interact with DPC micelles and these interactions initiate the formation of a second short α-helical region (Leu746-Asn756), which is not generally observed in either aqueous β3 or αIIbβ3 heterodimer" ... ". In this study, we also have accumulated the first direct evidence that tyrosine phosphorylation affects the structure and the association of 3CT with membrane."	DPC	SP	A-30-45	-	-	disorder to order	DisProt, DIBS	calculations, papers
P05106	2LJE	17931	set1	-	A	770	784	MemMoRF	intracellular	21956114	-	"Moreover, we have demonstrated that several residues of β3NP (Trp739, Thr741, Ala742, Pro745, and Tyr747) could interact with DPC micelles and these interactions initiate the formation of a second short α-helical region (Leu746-Asn756), which is not generally observed in either aqueous β3 or αIIbβ3 heterodimer" ... ". In this study, we also have accumulated the first direct evidence that tyrosine phosphorylation affects the structure and the association of 3CT with membrane."	DPC	SP	A-49-63	-	-	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05106	2LJF	17932	set1	-	A	751	766	MemMoRF	intracellular	21956114	-	"Moreover, we have demonstrated that several residues of β3NP (Trp739, Thr741, Ala742, Pro745, and Tyr747) could interact with DPC micelles and these interactions initiate the formation of a second short α-helical region (Leu746-Asn756), which is not generally observed in either aqueous β3 or αIIbβ3 heterodimer" ... ". In this study, we also have accumulated the first direct evidence that tyrosine phosphorylation affects the structure and the association of 3CT with membrane."	aqueous conditions	SP	A-30-45	-	-	disorder to order	DisProt, DIBS	calculations, papers
P05106	2LJF	17932	set1	-	A	770	784	MemMoRF	intracellular	21956114	-	"Moreover, we have demonstrated that several residues of β3NP (Trp739, Thr741, Ala742, Pro745, and Tyr747) could interact with DPC micelles and these interactions initiate the formation of a second short α-helical region (Leu746-Asn756), which is not generally observed in either aqueous β3 or αIIbβ3 heterodimer" ... ". In this study, we also have accumulated the first direct evidence that tyrosine phosphorylation affects the structure and the association of 3CT with membrane."	aqueous conditions	SP	A-49-63	-	-	disorder to order	DisProt, DIBS, calculations	calculations, papers
P05878	2M8M	19262	set1	-	A	656	683	MemMoRF	extracellular	24429284	-	"At the end of the simulation (235 ns) the peptide adopted a continuous helix, whose main axis was parallel to the lipid bilayer plane. In this state, the membraneinterface- embedded side-chains made contact preferentially with the polar head-groups of POPC, but not with Chol or PA."	hexafluoroisopropanol/water	SP	-	-	A-30-50	disorder to order	papers	papers
P05878	2M8O	19263	set1	-	A	656	683	MemMoRF	extracellular	24429284	-	"At the end of the simulation (235 ns) the peptide adopted a continuous helix, whose main axis was parallel to the lipid bilayer plane. In this state, the membraneinterface- embedded side-chains made contact preferentially with the polar head-groups of POPC, but not with Chol or PA."	DPC	SP	-	-	A-30-50	disorder to order	papers	papers
P06213	2MFR	19568	set1	-	A	942	948	MemMoRF	extracellular	24440425	-	"The residues 942–948 preceding the TMD have a propensity to be a short helix and may interact with membrane."	DPC	SP	A-4-10	Only available structure for this region.	A-19-41	disorder to order	calculations	calculations, papers
P07766	-	-	-	-	-	188	199	MemMoRF	intracellular	25992726	-	"Our results are also supported by the findings of Duchart et al. (3) in the structure of the TCR ζ chain. In solution, the cytoplasmic tail was unstructured. However, upon binding to lipid micelles, the peptide exhibited changes in the configuration, as is evident by the change in the chemical shift of the peptide. Here, we also observed that the conserved ITAM tyrosines are buried and interacting with the hydrophobic region of a negatively charged membrane, in line with the nuclear Overhauser effect measurements (10)."	-	SP	-	-	-	disorder to order	DisProt, DIBS, papers	papers
P07766	-	-	-	-	-	188	199	MemMoRF	intracellular	19733547	-	"Here we analyzed membrane binding of intrinsically disorderedζcyt, CD3εcyt, and FcRγcyt, and found that there are two different modes of their lipid-binding activity toward acidic phospholipids (Figs. 3b and S2c): 1) coupled binding and folding that is characteristic for micelles and those vesicles that are unstable upon protein binding (DMPG), and 2) binding without folding that is observed in the presence of stable vesicles (POPG)."	POPG LUV, POPG SUV	SP	-	Disorder to order in LMPG micelles, DMPG SUV, DMPG LUV and disorder to disorder in POPG LUV, POPG SUV.	-	disorder to order	DisProt, DIBS, papers	papers
P08411	1FW5	-	-	-	A	246	264	MemMoRF	intracellular	10984480	-	"The peptide interacted with liposomes only if negatively charged lipids were present that induced a structural change in the peptide from a random coil to a partially a-helical conformation. NMR structure shows that the a-helix is amphipathic, the hydrophobic surface consisting of several leucines, a valine, and a tryptophan moiety (Trp-259)."	-	-	A-2-20	-	-	disorder to order	papers	papers
P08514	1DPK	-	-	-	A	1020	1028	MemMoRF	intracellular	10677482	-	"As a comparison, although the nonmyristoylated aIIb-wt dissolved in DPC also exhibits the helical dNN(i,i11) NOEs in the N-terminal K989–R997 region,"	DPC micelle	SP	A-1-9	-	-	disorder to order	DisProt, papers	papers
P08514	1DPQ	-	-	-	A	1020	1028	MemMoRF	intracellular	10677482	-	"As a comparison, although the nonmyristoylated aIIb-wt dissolved in DPC also exhibits the helical dNN(i,i11) NOEs in the N-terminal K989–R997 region,"	DPC micelle	SP	A-1-9	-	-	disorder to order	DisProt, papers	papers
P08514	1M8O	-	-	-	-	1020	1028	MemMoRF	intracellular	12230976	-	-	DPC micelle	SP	-	-	-	disorder to order	DisProt, papers	papers
P08514	1S4W	-	-	-	A	1020	1028	MemMoRF	intracellular	15024114	-	"We show here that, whereas membrane-proximal helices of integrin α/β cytoplasmic tails associate in cytoplasm-like aqueous medium, they become partially embedded into membranemimetic micelles when unclasped" ... "Surprisingly, DPC induced substantial spectral changes for both nonmyristoylated αIIb and β3 tails (Fig. 2), demonstrating that each of the tail peptides bound to DPC. Resonance assignments of αIIb showed that only its membrane-proximal K989-R997 region is substantially perturbed on binding to DPC (Fig. 2 A), indicating that this region is involved in interacting with membrane."	DPC micelle	SP	A-1-9	-	-	disorder to order	DisProt, papers	papers
P08514	2K1A	-	-	-	A	1020	1028	MemMoRF	intracellular	18417472	-	"The structure is characterized by a linear α-helix for Ile-966–Lys-989 followed by a reversal of backbone direction that conversely immerses Phe-992–Phe-993 toward the lipid hydrocarbon core of the intracellular membrane face"	POPC:DHPC	SP	A-35-43	-	A-7-32	disorder to order	DisProt, papers	papers
P08514	2K9J	16497	set1	entity1	A	1020	1028	MemMoRF	intracellular	19279667	-	"the αIIb protection pattern nicely illustrates the αIIb(G991‐F992‐F993) backbone reversal and lipid re‐immersion of the two phenylalanine side chains in both monomeric and heterodimeric states. Compared with monomeric αIIb, the heterodimeric αIIb state showed a detectable increase in protection at the N‐terminal TM helix side and a decrease in protection C‐terminal to the TM helix (V990‐G991)." ... "At this point, it is noted that, in the absence of lipid environments, helical conformations for the αIIb(G991‐F992‐F993) sequence, which is fully conserved among all 18 integrin α subunits (Figure 1), were reported (Vinogradova et al, 2002; Weljie et al, 2002)."	isotropic bicelles (DHPC,POPC,POPS)	SP	A-32-40	-	A-7-32	disorder to order	DisProt, papers	papers
P08514	2KNC	16496	set1	entity1	A	1020	1028	MemMoRF	intracellular	19805198	-	"At the TM-CT border, the spatial positions of the positively charged groups of αIIb K989/β3 K716 (Fig. 1D) suggest that they begin the cytoplasmic regions. However, it is possible that the side chains following membrane-proximal residues αIIb V990-F993, β3 L717-I721 are inserted into or anchored onto the membrane (Fig. 1D), which may stabilize the relative orientations of the TM helices." ... "In the cytoplasmic region, the αIIb 989KVGFFKR displays a helical conformation in our structure, in which αIIb 990VGF weakly contacts β3 I719 and αIIb R995 forms a salt-bridge with β3 D723. In contrast, in Lau et al. (6), the helix ends at αIIb V990 followed by an unusual left handed reverse turn" ... "different solvent systems (CD3CN/H2O vs. bicelles) in the 2 studies may have captured 2 different conformational states of an intrinsically flexible region. The overall topology of the CT clasp determined in CD3CN/H2O was found to be similar to the one determined in aqueous solution (Fig. S5) (7), suggesting that this clasp represents a native conformation in the aqueous cytoplasm."	organic solvent	SP	A-35-43	-	A-9-34	disorder to order	DisProt, papers	papers
P0A334	1F6G	-	-	-	A,B,C,D	1	20	MemMoRF	intracellular	11158168	-	"the NH2 terminus is an α-helix positioned at the lipid–water interface, and the sharp drop in NiEdda accessibility around residues 15 and 16 may suggest a point of full insertion into the membrane" ... ". Recent experiments have shown that deletion of the first 20 residues in KcsA is associated with a dramatic reduction in expression levels. This may indicate that, as in other membrane proteins, the NH2 terminus of KcsA contains signaling information important for the correct folding and targeting of the channel in the inner membrane" ... "The NH2 terminus forms an amphipathic α-helix at the membrane–water interface that protrudes away from the channel core, and does not interact with any other part of the channel"	-	MP	A-1-20;B-1-20;C-1-20;D-1-20	Missing residues in X-ray structures.	A-28-50;A-88-111;B-28-50;B-88-111;C-28-50;C-88-111;D-28-50;D-88-111	disorder to order	papers	papers, structures
P0A6M2	2K73	15966	set1	-	A	2	9	MemMoRF	intracellular	18922471	-	"A previously unreported N-terminal amphipathic helix H1 (aa 2–9) precedes TM1 and is parallel to the membrane surface."	DPC	MP	A-2-9	Missing residues in X-ray structures.	A-15-31;A-50-65;A-72-89;A-145-163	disorder to order	papers	calculations, papers, structures
P0A6M2	2K73	15966	set1	-	A	116	119	ordered	extracellular	18922471	-	"PL2 is followed by a short amphipathic helical segment (H2, aa 116–119), which resides in the lipid bilayer (see below)."	DPC	MP	A-116-119	-	A-15-31;A-50-65;A-72-89;A-145-163	bistable helix	none	calculations, papers, structures
P0A6M2	2LEG	17710	set1	entity2	B	116	119	ordered	extracellular	21938394	-	-	E. coli lipids	MP	B-116-119	-	B-15-31;B-50-65;B-72-89;B-145-163	bistable helix	none	calculations, papers, structures
P0A6M2	2ZUP	-	-	-	-	116	119	ordered	extracellular	19214188	-	"The structure of the ‘horizontal helix’ revealed its clear amphiphilicity." ... "Taken together, we conclude that the hydrophobic side of the horizontal helix is associated with the membrane and that this association is important for DsbB activity to oxidize DsbA effectively."	-	MP	B-116-119	-	B-15-31;B-50-65;B-72-89;B-145-163	bistable helix	none	calculations, papers, structures
P0A734	-	-	-	-	-	2	9	MemMoRF	intracellular	21738659	-	"We have provided direct evidence that the extreme N-terminus of MinE from E. coli folds into an amphipathic α-helix when associated with a membrane. This property differed from MinE from Neisseria gonorrhoeae (Ng), which showed a stable N-terminal helix in solution [21]"	-	-	-	MinD and BDLP share common features of self-assembly on the membrane and nucleotide-mediated conformational changes; however, BDLP is anchored to the membrane by a hydrophobic paddle, while MinD is attached by an amphipathic helix.	-	disorder to order	papers	papers
P0ABN1	2KDC	-	-	-	A,B,C	7	24	ordered	intracellular	19556511	-	"motions associated with the N terminus (residues 1 to 25) have hindered determination of its conformation beyond confirming the presence of two stable amphipathic helices."	DPC	MP	A-6-23;B-6-23;C-6-23	X-ray structures shows the N-terminal amphiphilic helix.	A-33-48;A-52-68;A-95-118;B-33-48;B-52-68;B-95-118;C-33-48;C-52-68;C-95-118	bistable helix	none	papers, structures
P0C0Y1	1DX7	4303	set1	-	A	5	25	MemMoRF	intracellular	10756106	-	"Here, we present the solution structure of the LH1β polypeptide from Rb. sphaeroides in organic solvent along with that of a mutant deficient in a hydrogen bond to the Bchl co-factor termed W+9F. Our preliminary work on the wild-type polypeptide (Kikuchi et al., 1999) illustrated its helical nature and also showed that the structure in organic solvents is the same as in detergent micelles."	organic solvent	SP	A-4-24	Our calculations shows that the N-terminal helix is rather flexible and has low helix propensity in it's C-terminal half.	-	disorder to order	DisProt	papers, structures
P0C0Y1	1JO5	-	-	-	A	5	25	MemMoRF	intracellular	11772000	-	"The N-terminal amphipathic helix lies partially embedded in the micelle surface at an approximately 60° angle relative to the C-terminal helix which is inserted into the detergent micelle (Figure 6C)." ... "The data presented here support interactions of the charged face with Zwittergent 3:12's charged headgroups and the hydrophobic face with the micelle interior. So, in the Zwittergent 3:12 micelle, the C-terminal helix traverses the core of the micelle, the N-terminal helix lies along the micelle surface, and a hinge is required to connect the two." ... "The protein also seems to adopt a better defined fold in detergent micelles."	Zwittergent 3:12 micelles	SP	A-4-24	-	-	disorder to order	DisProt	papers, structures
P0C0Y1	-	-	-	-	A	5	25	MemMoRF	intracellular	10101971	-	"A comparison of CD spectra of LH1β observed in organic solvents and detergent micelles shows that the helical character of the peptide does not change appreciably between the two milieus."	-	SP	-	-	-	disorder to order	DisProt	papers, structures
P0DOF5	2RLF	-	-	-	A,B,C,D	51	59	ordered	intracellular	18235503	-	"a short flexible loop (residues 47–50) and a C-terminal amphipathic helix (residues 51– 59). The orientation and amphipathic character of the amphipathic helices suggest that the C-terminal base lies on the surface of the membrane."	DHPC	SP	A-34-42;B-34-42;C-34-42;D-34-42	-	-	bistable helix	none	papers, structures
P0DOF5	2N70	-	-	-	-	51	59	ordered	intracellular	19383794	-	"At the C-terminal base, the hydrophilic residues of the amphipathic helix are positioned to interact with the hydrophilic head groups of the lipids."	DPhPC	SP	-	-	-	bistable helix	none	papers, structures
P0DOF5	2KWX	-	-	-	-	51	59	ordered	intracellular	20833142	-	-	DHPC	SP	-	-	-	bistable helix	none	papers, structures
P0DOF5	2L0J	-	-	-	-	51	59	ordered	intracellular	20966252	-	"A third native-like aspect of the amphipathic helix is the outward projection of the charged residues Lys49, Arg53, His57, Lys60, and Arg61 (Fig. 1B), which conforms to the “positive inside rule” such that M2 interacts favorably with negatively charged lipids in native membranes." ... "Contrary to the lipid interfacial location determined here, the detergent-solubilized structure has the four amphipathic helices forming a bundle in the bulk aqueous solution where the amides fully exchange with deuterium"	DOPC:DOPE bicelles	SP	-	-	-	bistable helix	none	papers, structures
P10279	1SKH	-	-	-	A	10	17	MemMoRF	intracellular	15554701	-	"The sequence of the bPrPp differs from the typical amphipathic properties seen in, e.g., penetratin and instead contains a stretch of hydrophobic residues (Ile10−Met17). This is likely to affect the properties of the bPrPp peptide as a CPP and make it less benign than, e.g., penetratin in its membrane interactions. This property could possibly be related to toxicity coupled to membrane translocation in the biological effects of bPrP and its potential cargo comprised of the remainder of the PrP."	DHPC	-	-	-	-	disorder to order	PFAM	papers
P10636	5N5A	-	-	-	A	570	577	MemMoRF	intracellular	29215007	-	"Tau residues 253–260, 315–322, and 345–354 populate helical structure in the presence of detergent and upon binding to membranes65" … "Thus, when both F-actin and microtubules are present, they would compete for binding to residues 245–246, 275–284, and 305–313, while Tau residues 259–267, 289–297, and 320–330 will preferentially interact with F-actin"	-	-	A-1-8	-	-	disorder to order	papers	papers
P10636	5N5B	-	-	-	A	632	639	MemMoRF	intracellular	29215007	-	"Tau residues 253–260, 315–322, and 345–354 populate helical structure in the presence of detergent and upon binding to membranes65" … "Thus, when both F-actin and microtubules are present, they would compete for binding to residues 245–246, 275–284, and 305–313, while Tau residues 259–267, 289–297, and 320–330 will preferentially interact with F-actin"	-	-	A-24-28	-	-	disorder to order	papers	papers
P10636	5N5B	-	-	-	A	662	671	MemMoRF	intracellular	29215007	-	"Tau residues 253–260, 315–322, and 345–354 populate helical structure in the presence of detergent and upon binding to membranes65" … "Thus, when both F-actin and microtubules are present, they would compete for binding to residues 245–246, 275–284, and 305–313, while Tau residues 259–267, 289–297, and 320–330 will preferentially interact with F-actin"	-	-	-	-	-	disorder to order	papers	papers
P10636	5NVB	-	-	-	A	570	577	MemMoRF	intracellular	29215007	-	"Tau residues 253–260, 315–322, and 345–354 populate helical structure in the presence of detergent and upon binding to membranes65" … "Thus, when both F-actin and microtubules are present, they would compete for binding to residues 245–246, 275–284, and 305–313, while Tau residues 259–267, 289–297, and 320–330 will preferentially interact with F-actin"	-	-	A-1-8	-	-	disorder to order	papers	papers
P10636	-	-	-	-	A	570	577	MemMoRF	intracellular	16908029	-	"We find that micelle-associated tau K19 adopts three segments of highly helical structure, consisting of residues 253−261, 315−323, and 346−355, as indicated by chemical shift and scalar coupling data with further support from relaxation and NOE measurements. These three helices exactly superimpose on the three regions with the strongest indications for nascent helical structure that we previously identified in our studies of the tau K19 polypeptide free in solution.52"	SDS	-	-	-	-	disorder to order	papers	papers
P10636	-	-	-	-	-	570	577	MemMoRF	intracellular	2522951	-	"Tau K19 binds to unilamellar 1:1 POPC/POPS lipid vesicles, and the segments comprising residues 253–261, 315–323, and 346–355 adopt a highly helical structure" … "The helices in the tau MBD repeats are located at the membrane surface and do not penetrate deeply into the lipid bilayer"	-	-	-	-	-	disorder to order	papers	papers
P10636	-	-	-	-	A	632	639	MemMoRF	intracellular	16908029	-	"We find that micelle-associated tau K19 adopts three segments of highly helical structure, consisting of residues 253−261, 315−323, and 346−355, as indicated by chemical shift and scalar coupling data with further support from relaxation and NOE measurements. These three helices exactly superimpose on the three regions with the strongest indications for nascent helical structure that we previously identified in our studies of the tau K19 polypeptide free in solution.52"	SDS	-	-	-	-	disorder to order	papers	papers
P10636	-	-	-	-	-	632	639	MemMoRF	intracellular	2522951	-	"Tau K19 binds to unilamellar 1:1 POPC/POPS lipid vesicles, and the segments comprising residues 253–261, 315–323, and 346–355 adopt a highly helical structure" … "The helices in the tau MBD repeats are located at the membrane surface and do not penetrate deeply into the lipid bilayer"	-	-	-	-	-	disorder to order	papers	papers
P10636	-	-	-	-	A	662	671	MemMoRF	intracellular	16908029	-	"We find that micelle-associated tau K19 adopts three segments of highly helical structure, consisting of residues 253−261, 315−323, and 346−355, as indicated by chemical shift and scalar coupling data with further support from relaxation and NOE measurements. These three helices exactly superimpose on the three regions with the strongest indications for nascent helical structure that we previously identified in our studies of the tau K19 polypeptide free in solution.52"	SDS	-	-	-	-	disorder to order	papers	papers
P10636	-	-	-	-	A	662	671	MemMoRF	intracellular	16908029	-	"We find that micelle-associated tau K19 adopts three segments of highly helical structure, consisting of residues 253−261, 315−323, and 346−355, as indicated by chemical shift and scalar coupling data with further support from relaxation and NOE measurements. These three helices exactly superimpose on the three regions with the strongest indications for nascent helical structure that we previously identified in our studies of the tau K19 polypeptide free in solution.52"	SDS	-	-	-	-	disorder to order	papers	papers
P10636	-	-	-	-	-	662	671	MemMoRF	intracellular	2522951	-	"Tau K19 binds to unilamellar 1:1 POPC/POPS lipid vesicles, and the segments comprising residues 253–261, 315–323, and 346–355 adopt a highly helical structure" … "The helices in the tau MBD repeats are located at the membrane surface and do not penetrate deeply into the lipid bilayer"	-	-	-	-	-	disorder to order	papers	papers
P10912	-	-	-	-	-	270	357	MemMoRF	intracellular	25846210	-	"the human prolactin (PRL) receptor (PRLR) and growth hormone receptor (GHR) ICDs are intrinsically disordered throughout their entire lengths. We show that they interact specifically with hallmark lipids of the inner plasma membrane leaflet through conserved motifs resembling immuno receptor tyrosine-based activation motifs (ITAMs). However, contrary to the observations made for ITAMs, lipid association of the PRLR and GHR ICDs was shown to be unaccompanied by changes in transient secondary structure and independent of tyrosine phosphorylation." ... "Importantly, we noticed that the structural elements located in LID1 and LID3 of the PRLR-ICD were conserved in the GHR-ICD (Figure 3E), suggesting that they may be important for the lipid association [13]" ... "Combined, these data showed that the PRLR and GHR ICDs were intrinsically disordered and interacted with hallmark lipids of the inner plasma membrane leaflet through a highly conserved LID1 in a manner not accompanied by induced folding (Supplementary Figure S4)."	POPC/POPS SUVs	SP	-	-	-	disorder to disorder	DisProt, papers	papers
P10997	2KB8	-	-	-	A	53	61	MemMoRF	extracellular	19244249	-	"The spin probe data suggest that the segment between residues 5 and 17 is positioned within the hydrophobic lipid environment, whereas the amyloidogenic segment between residues 20 and 29 is at the interface between the lipid and solvent. This orientation may direct the aggregation of amylin on membranes, whereas coupling between the two segments may mediate the transition to a toxic structure." ... "Presumably, aggregation of the amyloidogenic 20–29-residue segment results in the transmission of a conformational switch to the 5–17-residue segment that allows it to traverse the membrane bilayer. Structural coupling between the amyloidogenic and membrane-immersed segments could thus facilitate the transition to a toxic state when membrane-bound amylin oligomerizes." ... "Although amylin can bind to phospholipids as a monomer (58), we are unaware of such an interaction in the normal function of amylin. At the same time amylin needs to bind to transmembrane receptors (59) and to cross the blood-brain barrier (60) so the hydrophobic character of the N-terminal part of the hormone could facilitate those functions."	SDS	-	A-20-28	-	-	disorder to order	papers	papers
P10997	2L86	-	-	-	A	38	52	ordered	extracellular	21723249	-	"The structure has an overall kinked helix motif, with residues 7-17 and 21-28 in a helical conformation, and with a 3(10) helix from Gly 33-Asn 35."	SDS	-	A-5-19	-	-	bistable helix	none	papers
P10997	2L86	-	-	-	A	53	61	MemMoRF	extracellular	21723249	-	"The structure has an overall kinked helix motif, with residues 7-17 and 21-28 in a helical conformation, and with a 3(10) helix from Gly 33-Asn 35."	SDS	-	A-20-28	-	-	disorder to order	papers	papers
P10997	5MGQ	-	-	-	A	38	52	ordered	extracellular	28287098	-	"Initially, it was suggested that hIAPP adopts a random coil structure23. However, more recently reports indicate that the N-terminal part of hIAPP involving residues 5–19 and to a somewhat smaller degree residues 20–22 transiently samples an α-helical structure in solution8,24. The same residues adopt a fully helical structure when bound to membranes or micelles19,24,25"	aqueous	-	A-5-19	-	-	bistable helix	none	papers
P12931	-	-	-	-	-	60	67	MemMoRF	intracellular	23416516	-	"Significant shifts were observed in two regions: the N-terminal SH4 domain and residues S51, A53, A55, and 60EPKLFGGF67 of the Unique domain. The observed shifts in the Unique domain region were larger than those observed in the well known lipid binding SH4 domain. The 60–67 segment is included in the partially structured region (60–75) previously determined by NMR17 and we refer to it as the Unique Lipid Binding Region (ULBR). The SH4 domain and the ULBR showed affinity for negatively charged lipids. However, in contrast to residues in the SH4 domain, the ULBR was also substantially perturbed by neutral lipid bicelles. The specificity for different lipid classes was tested using Lipid-StripsTM. USrc binds preferentially to acidic lipids, namely phosphatidic acid (PA), cardiolipin (CL), phosphatidylserine (PS), phosphatidylinositol-4-phosphate (PtdIns(4)P), and phosphatidylinositol-3,4,5-triphosphate (PtdIns(3,4,5)P3) (Fig. 1c)."	-	-	-	-	-	disorder to order	DisProt, papers	papers
P12931	-	-	-	-	-	98	102	MemMoRF	intracellular	23416516	-	"We demonstrate, for the first time, that human c-Src has at least two additional lipid binding regions in addition to the SH4 domain that show specificity for acidic lipids, including phosphoinositides." ... "The second one includes residues in the RT and nSrc loops of the SH3 domain."	-	-	-	-	-	disorder to order	papers	papers
P12931	-	-	-	-	-	12	19	MemMoRF	intracellular	25914053	-	"PPP binding nearly completely abolished direct lipid interaction of the SH3domain but preserved those of residues 64–67 (ULBR) and 14–17 in the C-terminal part of the SH4 domain." ... "Residues 12–19 constitute the cSH4 subdomain that shows the largest perturbations in the presence of nega-tively charged lipids."	-	-	-	See also https://doi.org/10.1016/S1063-5823(02)52012-3	-	disorder to disorder	DisProt, papers	papers
P12969	2KJ7	-	-	-	A	55	60	MemMoRF	extracellular	19456151	-	"The structure of rIAPP in DPC micelles is dominated by a N-terminal helical region from residues A5 to S23 and a disordered C-terminus. In solution, the helical region of rIAPP is shorter than in the membrane-bound form, spanning residues 5–19, whereas residues 20–23 are involved in hydrogen-bonding interactions with the helix but do not adopt a helical conformation." ... "It is interesting to note that the decrease in the intensity of the α-proton chemical shift resonances upon the addition of the quencher is less in the stable helix located toward the N-terminal region (A5–V17) than in the flexible but structured helix (R18–L23) and the unstructured C-terminus (G24–Y37), indicating that the C-terminal region is significantly more exposed to the solvent. Thus, the site-specific paramagnetic quenching results clearly indicate that the N-terminal part of rat IAPP is a stable helix that is bound to the surface of the membrane, whereas the C-terminal is mobile and is exposed to the solvent,"	DPC	-	A-18-23	rIAPP dos not form toxic amyloid plakks like human IAPP.	-	disorder to order	papers	papers
P15382	2K21	15102	set1	-	A	12	23	MemMoRF	extracellular	18611041	-	"This model reflects the amphipathicity of the helix spanning residues 12-23 and the presence of a net positive charge for the helix spanning residues 92-106, properties that confer affinity for the negatively charged surface of LMPG micelles."	LMPG	SP	A-21-32	-	-	disorder to order	calculations	papers
P15382	2K21	15102	set1	-	A	92	106	MemMoRF	intracellular	18611041	-	"This model reflects the amphipathicity of the helix spanning residues 12-23 and the presence of a net positive charge for the helix spanning residues 92-106, properties that confer affinity for the negatively charged surface of LMPG micelles."	LMPG	SP	A-101-115	-	-	disorder to order	calculations	papers
P16471	-	-	-	-	-	260	300	MemMoRF	intracellular	25846210	-	"the human prolactin (PRL) receptor (PRLR) and growth hormone receptor (GHR) ICDs are intrinsically disordered throughout their entire lengths. We show that they interact specifically with hallmark lipids of the inner plasma membrane leaflet through conserved motifs resembling immuno receptor tyrosine-based activation motifs (ITAMs). However, contrary to the observations made for ITAMs, lipid association of the PRLR and GHR ICDs was shown to be unaccompanied by changes in transient secondary structure and independent of tyrosine phosphorylation." ... "Collectively, these data showed that the PRLR-ICD interacted specifically with negatively charged inner leaflet lipids through three LIDs; LID1 (Gly236–His300), LID2 (Phe350–His383) and LID3 (Cys547–His598). These LIDs contained four of the identified THs (TH1–TH3 and TH5), but no changes in secondary structure were observed from CD analyses upon POPC/POPS SUV binding for PRLR-ICDFL, PRLR-ICDmp or PRLR-ICDmd (Supplementary Figures S4A–S4C)."	POPC/POPS SUVs	SP	-	-	-	disorder to disorder	DisProt, papers	papers
P16471	-	-	-	-	-	350	383	MemMoRF	intracellular	25846210	-	"the human prolactin (PRL) receptor (PRLR) and growth hormone receptor (GHR) ICDs are intrinsically disordered throughout their entire lengths. We show that they interact specifically with hallmark lipids of the inner plasma membrane leaflet through conserved motifs resembling immuno receptor tyrosine-based activation motifs (ITAMs). However, contrary to the observations made for ITAMs, lipid association of the PRLR and GHR ICDs was shown to be unaccompanied by changes in transient secondary structure and independent of tyrosine phosphorylation." ... "Collectively, these data showed that the PRLR-ICD interacted specifically with negatively charged inner leaflet lipids through three LIDs; LID1 (Gly236–His300), LID2 (Phe350–His383) and LID3 (Cys547–His598). These LIDs contained four of the identified THs (TH1–TH3 and TH5), but no changes in secondary structure were observed from CD analyses upon POPC/POPS SUV binding for PRLR-ICDFL, PRLR-ICDmp or PRLR-ICDmd (Supplementary Figures S4A–S4C)."	POPC/POPS SUVs	SP	-	-	-	disorder to disorder	DisProt, papers	papers
P16471	-	-	-	-	-	547	598	MemMoRF	intracellular	25846210	-	"the human prolactin (PRL) receptor (PRLR) and growth hormone receptor (GHR) ICDs are intrinsically disordered throughout their entire lengths. We show that they interact specifically with hallmark lipids of the inner plasma membrane leaflet through conserved motifs resembling immuno receptor tyrosine-based activation motifs (ITAMs). However, contrary to the observations made for ITAMs, lipid association of the PRLR and GHR ICDs was shown to be unaccompanied by changes in transient secondary structure and independent of tyrosine phosphorylation." ... "Collectively, these data showed that the PRLR-ICD interacted specifically with negatively charged inner leaflet lipids through three LIDs; LID1 (Gly236–His300), LID2 (Phe350–His383) and LID3 (Cys547–His598). These LIDs contained four of the identified THs (TH1–TH3 and TH5), but no changes in secondary structure were observed from CD analyses upon POPC/POPS SUV binding for PRLR-ICDFL, PRLR-ICDmp or PRLR-ICDmd (Supplementary Figures S4A–S4C)."	POPC/POPS SUVs	SP	-	-	-	disorder to disorder	DisProt, papers	papers
P17810	-	-	-	-	-	310	325	MemMoRF	intracellular	28325841	-	"in vitro studies show that the P/rds C terminus is intrinsically disordered, but membrane mimetics can induce helical structure in its central region" ... "the central portion of this domain can partition into phospholipid membranes as an AH and can specifically participate in (but is not required for) membrane curvature generation."	LUV: POPG, POPC, DOPC, DOPE, DOPS	MP	-	-	-	disorder to order	DisProt, papers	papers
P19235	2MV6	25079	set1	-	A	240	244	MemMoRF	extracellular	25418301	-	"Although the N-terminal residues of the construct are not structured, some residues are protected from exposure to Gd-DTPA, suggesting that this region may interact with micelles."	DPC	SP	A-5-9	-	A-16-38	disorder to disorder	calculations, papers	papers
P19836	1PEH	-	-	-	A	243	266	MemMoRF	intracellular	8810902	-	"In water, the CD spectra of the CT peptides were indicative of predominently random coil conformation" ... "However, in the presence of anionic amphiphiles such as SDS they adopted a predominently a-helical structure (Figure 2)."	SDS	-	A-9-32	Missing residues from X-ray structures.	-	disorder to order	DisProt, papers	papers
P19836	-	-	-	-	-	243	266	MemMoRF	intracellular	23238251	-	"The lipid compositional sensor is a lipid-inducible amphipathic helix, domain M. Although the regulation and mechanisms of membrane binding of domain M are well understood,11,12" ... "CD data,19 disorder predictions,[17], [23] and the inter-subunit disulfide bridging and unfocussed intra-domain M BBP cross-linking data we presented here for rat CCT argue against a stable α-helical structure for the entire M domain in the soluble form but are compatible with a small, pre-folded α-helical segment (e.g., the primary AI motif) on a flexible leash."	DOPG, PC, PG	-	-	Amphitropic protein.	-	disorder to order	DisProt, papers	papers
P20444	-	-	-	-	-	625	634	MemMoRF	intracellular	23762412	-	"We show that V5α and its phosphorylation-mimicking variant, dmV5α, are intrinsically disordered protein domains ." ... "Upon micelle binding, V5α acquires a higher propensity to form helical structures at the conserved "NFD" motif and the entire C-terminal third of the domain."	-	-	-	-	-	disorder to order	DisProt, papers	papers
P20963	-	-	-	-	-	111	126	MemMoRF	intracellular	17410622	-	"ITAM1 is unstructured and not associated with the micelle. On the other hand, for ITAM3, the capacity to form an amphiphilic helix is in agreement with our finding that this region interacts with the detergent micelle and that it has to be a-helical." ... "chemical-shift analysis demonstrated that z is intrinsically unfolded in solution." ... "Consequently, the detected a-helical content of the TCRz-chain upon micelle binding has to be located within the un-assignable, broadened regions at the second and third ITAM motif."	LMPG micelle	SP	-	-	-	disorder to order	DisProt, papers	papers
P20963	-	-	-	-	-	142	156	MemMoRF	intracellular	17410622	-	"ITAM1 is unstructured and not associated with the micelle." ... "For ITAM2, it is apparent that italso associates with the membrane" ... "chemical-shift analysis demonstrated that z is intrinsically unfolded in solution." ... "Consequently, the detected a-helical content of the TCRz-chain upon micelle binding has to be located within the un-assignable, broadened regions at the second and third ITAM motif."	LMPG micelle	SP	-	-	-	disorder to order	DisProt, DIBS, papers	papers
P20963	-	-	-	-	-	111	126	MemMoRF	intracellular	11062556	-	"In aqueous solution, zeta(cyt) is unstructured. Here we report that in the presence of lipid vesicles zeta(cyt) assumes a folded structure. The folding transition is reversible and dependent on the presence of acidic phospholipids." ... "Lipid binding regulates ζcyt phosphorylation"	Synthetic lipids (DMPC, DMPG, DMPS, DMPA), purified natural lipids (PI, PIP, PIP2) from bovine liver, or lipid mixtures	SP	-	-	-	disorder to order	DisProt, papers	papers
P20963	-	-	-	-	-	111	126	MemMoRF	intracellular	22084078	-	"the C terminus of TCRζcyt is closely associated with the plasma membrane and this association is dependent on BRS motifs; (ii) TCR engagement induces dissociation of the TCRζcyt from the plasma membrane and this dissociation requires TCRζcyt phosphorylation;"	-	SP	-	-	-	disorder to order	DisProt, papers	papers
P20963	-	-	-	-	-	111	126	MemMoRF	intracellular	19733547	-	"Here we analyzed membrane binding of intrinsically disorderedζcyt, CD3εcyt, and FcRγcyt, and found that there are two different modes of their lipid-binding activity toward acidic phospholipids (Figs. 3b and S2c): 1) coupled binding and folding that is characteristic for micelles and those vesicles that are unstable upon protein binding (DMPG), and 2) binding without folding that is observed in the presence of stable vesicles (POPG)."	POPG LUV, POPG SUV / LMPG micelles, DMPG SUV, DMPG LUV	SP	-	POPG LUV, POPG SUV : disorder to disorder. LMPG micelles, DMPG SUV, DMPG LUV : disorder to order.	-	disorder to order	DisProt, papers	papers
P20963	-	-	-	-	-	142	156	MemMoRF	intracellular	11062556	-	"In aqueous solution, zeta(cyt) is unstructured. Here we report that in the presence of lipid vesicles zeta(cyt) assumes a folded structure. The folding transition is reversible and dependent on the presence of acidic phospholipids." ... "Lipid binding regulates ζcyt phosphorylation"	Synthetic lipids (DMPC, DMPG, DMPS, DMPA), purified natural lipids (PI, PIP, PIP2) from bovine liver, or lipid mixtures	SP	-	-	-	disorder to order	DisProt, DIBS, papers	papers
P20963	-	-	-	-	-	142	156	MemMoRF	intracellular	22084078	-	"the C terminus of TCRζcyt is closely associated with the plasma membrane and this association is dependent on BRS motifs; (ii) TCR engagement induces dissociation of the TCRζcyt from the plasma membrane and this dissociation requires TCRζcyt phosphorylation;"	-	SP	-	-	-	disorder to order	DisProt, DIBS, papers	papers
P20963	-	-	-	-	-	142	156	MemMoRF	intracellular	19733547	-	"Here we analyzed membrane binding of intrinsically disorderedζcyt, CD3εcyt, and FcRγcyt, and found that there are two different modes of their lipid-binding activity toward acidic phospholipids (Figs. 3b and S2c): 1) coupled binding and folding that is characteristic for micelles and those vesicles that are unstable upon protein binding (DMPG), and 2) binding without folding that is observed in the presence of stable vesicles (POPG)."	LMPG micelles, DMPG SUV, DMPG LUV	SP	-	POPG LUV, POPG SUV : disorder to disorder. LMPG micelles, DMPG SUV, DMPG LUV : disorder to order.	-	disorder to order	DisProt, DIBS, papers	papers
P21579	-	-	-	-	-	80	90	MemMoRF	intracellular	27191789	-	"we first sought conditions under which the IDR may become partially ordered and found that the lipid composition of the membrane was a key factor. In the presence of a complex lipid mixture that mimics the outer leaflet of a synaptic vesicle (Figure 1B), we found through DSC (Figure 2) and NMR (Figure 4) measurements that the IDR experiences endotherm and chemical shift changes, respectively, consistent with IDR–synaptic lipid interactions, though in a mostly disordered structural state."	-	SP	-	-	-	disorder to disorder	papers	papers
P22646	2K4F	-	-	-	A	169	173	MemMoRF	intracellular	19013279	-	"the long N-terminal segment is highly flexible, while the close interaction of the hydrophobic residues of the ITAM with the lipid induces partial folding of the ITAM centered on the critical residues of the motif."	-	SP	A-37-41	-	-	disorder to order	PFAM, papers	papers
P22646	2K4F	-	-	-	A	181	185	MemMoRF	intracellular	19013279	-	"the long N-terminal segment is highly flexible, while the close interaction of the hydrophobic residues of the ITAM with the lipid induces partial folding of the ITAM centered on the critical residues of the motif."	-	SP	A-49-53	-	-	disorder to order	papers	papers
P22943	2L9Q	17482	set1	-	A	9	18	MemMoRF	intracellular	21998307	-	"Secondary structural elements determined from assigned chemical shifts indicated that Hsp12 is dynamically disordered in aqueous solution, whereas it gains four helical stretches in the presence of SDS micelles and a single helix in presence of DPC" ... ". R(1) and R(2), relaxation and heteronuclear NOE measurements showed that the protein is disordered in aqueous solution but becomes more ordered in presence of detergent micelles. NMR spectra collected in presence of paramagnetic spin relaxation agents (5DSA, 16DSA, and Gd(DTPA-BMA)) indicated that the amphipathic α-helices of Hsp12 in SDS micelles lie on the membrane surface"	SDS	-	A-9-18	-	-	disorder to order	DisProt, papers	calculations, papers
P22943	2L9Q	17482	set1	-	A	22	42	MemMoRF	intracellular	21998307	-	"Secondary structural elements determined from assigned chemical shifts indicated that Hsp12 is dynamically disordered in aqueous solution, whereas it gains four helical stretches in the presence of SDS micelles and a single helix in presence of DPC" ... ". R(1) and R(2), relaxation and heteronuclear NOE measurements showed that the protein is disordered in aqueous solution but becomes more ordered in presence of detergent micelles. NMR spectra collected in presence of paramagnetic spin relaxation agents (5DSA, 16DSA, and Gd(DTPA-BMA)) indicated that the amphipathic α-helices of Hsp12 in SDS micelles lie on the membrane surface"	SDS	-	A-22-42	-	-	disorder to order	DisProt, papers	calculations, papers
P22943	2L9Q	17482	set1	-	A	52	63	MemMoRF	intracellular	21998307	-	"Secondary structural elements determined from assigned chemical shifts indicated that Hsp12 is dynamically disordered in aqueous solution, whereas it gains four helical stretches in the presence of SDS micelles and a single helix in presence of DPC" ... ". R(1) and R(2), relaxation and heteronuclear NOE measurements showed that the protein is disordered in aqueous solution but becomes more ordered in presence of detergent micelles. NMR spectra collected in presence of paramagnetic spin relaxation agents (5DSA, 16DSA, and Gd(DTPA-BMA)) indicated that the amphipathic α-helices of Hsp12 in SDS micelles lie on the membrane surface"	SDS	-	A-52-63	-	-	disorder to order	DisProt, papers	calculations, papers
P22943	2L9Q	17482	set1	-	A	74	100	MemMoRF	intracellular	21998307	-	"Secondary structural elements determined from assigned chemical shifts indicated that Hsp12 is dynamically disordered in aqueous solution, whereas it gains four helical stretches in the presence of SDS micelles and a single helix in presence of DPC" ... ". R(1) and R(2), relaxation and heteronuclear NOE measurements showed that the protein is disordered in aqueous solution but becomes more ordered in presence of detergent micelles. NMR spectra collected in presence of paramagnetic spin relaxation agents (5DSA, 16DSA, and Gd(DTPA-BMA)) indicated that the amphipathic α-helices of Hsp12 in SDS micelles lie on the membrane surface"	SDS	-	A-74-100	-	-	disorder to order	DisProt, papers	calculations, papers
P22943	2LJL	17948	set1	-	A	74	100	MemMoRF	intracellular	21998307	-	"Secondary structural elements determined from assigned chemical shifts indicated that Hsp12 is dynamically disordered in aqueous solution, whereas it gains four helical stretches in the presence of SDS micelles and a single helix in presence of DPC" ... ". R(1) and R(2), relaxation and heteronuclear NOE measurements showed that the protein is disordered in aqueous solution but becomes more ordered in presence of detergent micelles. NMR spectra collected in presence of paramagnetic spin relaxation agents (5DSA, 16DSA, and Gd(DTPA-BMA)) indicated that the amphipathic α-helices of Hsp12 in SDS micelles lie on the membrane surface"	DPC	-	A-74-100	-	-	disorder to order	DisProt, papers	calculations, papers
P22943	2LJL	17948	set1	-	A	22	42	MemMoRF	intracellular	21998307	-	-	DPC	-	A-74-100	-	-	disorder to order	DisProt, papers	calculations, papers
P22943	4AXP	-	-	-	A	9	18	MemMoRF	intracellular	22848679	-	"NMR analysis indicated that Hsp12 is monomeric and intrinsically unfolded in solution, but switches to a 4-helical conformation upon binding to membrane-mimetic SDS micelles. The structure of micelle-bound Hsp12 reported here is consistent with its recently proposed function as a membrane-stabilising 'lipid chaperone'. Taken together, our data suggest that DR-induced Hsp12 expression contributes to lifespan extension, possibly via membrane alterations."	SDS	-	A-9-18	-	-	disorder to order	DisProt, papers	calculations, papers
P22943	4AXP	-	-	-	A	22	42	MemMoRF	intracellular	22848679	-	"NMR analysis indicated that Hsp12 is monomeric and intrinsically unfolded in solution, but switches to a 4-helical conformation upon binding to membrane-mimetic SDS micelles. The structure of micelle-bound Hsp12 reported here is consistent with its recently proposed function as a membrane-stabilising 'lipid chaperone'. Taken together, our data suggest that DR-induced Hsp12 expression contributes to lifespan extension, possibly via membrane alterations."	SDS	-	A-22-42	-	-	disorder to order	DisProt, papers	calculations, papers
P22943	4AXP	-	-	-	A	52	63	MemMoRF	intracellular	22848679	-	"NMR analysis indicated that Hsp12 is monomeric and intrinsically unfolded in solution, but switches to a 4-helical conformation upon binding to membrane-mimetic SDS micelles. The structure of micelle-bound Hsp12 reported here is consistent with its recently proposed function as a membrane-stabilising 'lipid chaperone'. Taken together, our data suggest that DR-induced Hsp12 expression contributes to lifespan extension, possibly via membrane alterations."	SDS	-	A-52-63	-	-	disorder to order	DisProt, papers	calculations, papers
P22943	4AXP	-	-	-	A	74	100	MemMoRF	intracellular	22848679	-	"NMR analysis indicated that Hsp12 is monomeric and intrinsically unfolded in solution, but switches to a 4-helical conformation upon binding to membrane-mimetic SDS micelles. The structure of micelle-bound Hsp12 reported here is consistent with its recently proposed function as a membrane-stabilising 'lipid chaperone'. Taken together, our data suggest that DR-induced Hsp12 expression contributes to lifespan extension, possibly via membrane alterations."	SDS	-	A-74-100	-	-	disorder to order	DisProt, papers	calculations, papers
P26039	2KC2	-	-	-	A	144	167	MemMoRF	intracellular	20150896	-	"F1 loop interacts with negatively charged lipid bilayers" ... "An encounter between the loop and a cluster of negatively charged phospholipids on the cytoplasmic face of the membrane would induce the loop to adopt a folded helical structure in which basic residues on one side of the helix are bound to the membrane. This folding would decrease the length of the loop and draw the F1 domain closer to the membrane"	-	-	A-70-93	-	-	disorder to order	DisProt	papers
P26039	2KMA	-	-	-	A	144	167	MemMoRF	intracellular	20150896	-	"F1 loop interacts with negatively charged lipid bilayers" ... "An encounter between the loop and a cluster of negatively charged phospholipids on the cytoplasmic face of the membrane would induce the loop to adopt a folded helical structure in which basic residues on one side of the helix are bound to the membrane. This folding would decrease the length of the loop and draw the F1 domain closer to the membrane"	-	-	-	-	-	disorder to order	DisProt	papers
P26678	-	-	-	-	-	2	15	MemMoRF	intracellular	22381409	-	"the cytoplasmic domain of PLB (Ia and Ib) is in equilibrium between an ordered T state and a dynamically disordered (partially unfolded) R state" ... "We conclude that PLB binds to SERCA in two distinct structural states of the cytoplasmic domain, an inhibitory T state that interacts strongly with the membrane surface, and a less inhibitory R state that interacts more strongly with the anionic SERCA cytoplasmic domain." ... "Modulating membrane surface charge provides an effective way of investigating the correlation between structural dynamics and function of integral membrane proteins."	-	SP	-	-	-	disorder to order	papers	papers
P26678	1PLP	-	-	-	-	2	15	MemMoRF	intracellular	7779806	-	"This disruption of structure at the C-terminus of the helix suggests a model for phosphorylation-induced dissociation of the PLB/Ca*+-ATPase complex."	SDS	SP	A-2-16	-	A-32-52	disorder to order	papers	papers
P26678	1ZLL	-	-	-	-	2	15	MemMoRF	intracellular	16043693	-	"each subunit consists of a short, positively charged amphipathic (AP) α-helix (residues 2-15), an extended linker (residues 16-22) in which residues 18-20 acquire dihedral angles characteristic of β-strand," ... "These structural features suggest that PLN in the pentameric form can initiate binding of SERCA without having to dissociate first. Fig. 4 shows, however, that the original subunit conformation in the pentamer cannot simultaneously satisfy the distance restraints between PLN and SERCA that were derived from chemical crosslinking data, which include distances between K3, N27, and L49 of PLN and K400, L321, and V89 of SERCA, respectively (3, 36). To satisfy these contacts, a PLN subunit may have to be significantly stretched." ... "The phosphorylation sites S16 and/or T17 are located next to the joint of the AP helix and the strand"	DPC	SP	A-2-16;B-2-16;C-2-16;D-2-16;E-2-16	-	A-32-52;B-32-52;C-32-52;D-32-52;E-32-52	disorder to order	papers	papers
P27958	1R7C	-	-	-	A	1978	1998	MemMoRF	intramembrane	15247283	-	"An α-helix extending from amino acid residue 5 to 25 was observed in the presence of different membrane mimetic media. This helix exhibited a hydrophobic, Trp rich side embedded in detergent micelles, while the polar, charged side was exposed to the solvent. Thus, the NS5A membrane anchor domain forms an in-plane amphipathic α-helix embedded in the cytosolic leaflet of the membrane bilayer."	TFE	SP	A-6-26	-	A-1019-1039	disorder to order	papers	papers
P27958	1R7D	5978	set1	-	A	1978	1998	MemMoRF	intramembrane	15247283	-	"An α-helix extending from amino acid residue 5 to 25 was observed in the presence of different membrane mimetic media. This helix exhibited a hydrophobic, Trp rich side embedded in detergent micelles, while the polar, charged side was exposed to the solvent. Thus, the NS5A membrane anchor domain forms an in-plane amphipathic α-helix embedded in the cytosolic leaflet of the membrane bilayer."	TFE	SP	A-6-26	-	A-1019-1039	disorder to order	papers	papers
P27958	1R7E	5978	set2	-	A	1978	1998	MemMoRF	intramembrane	15247283	-	"An α-helix extending from amino acid residue 5 to 25 was observed in the presence of different membrane mimetic media. This helix exhibited a hydrophobic, Trp rich side embedded in detergent micelles, while the polar, charged side was exposed to the solvent. Thus, the NS5A membrane anchor domain forms an in-plane amphipathic α-helix embedded in the cytosolic leaflet of the membrane bilayer."	SDS	SP	A-6-26	-	A-1019-1039	disorder to order	papers	papers
P27958	1R7F	-	-	-	A	1978	1998	MemMoRF	intramembrane	15247283	-	"An α-helix extending from amino acid residue 5 to 25 was observed in the presence of different membrane mimetic media. This helix exhibited a hydrophobic, Trp rich side embedded in detergent micelles, while the polar, charged side was exposed to the solvent. Thus, the NS5A membrane anchor domain forms an in-plane amphipathic α-helix embedded in the cytosolic leaflet of the membrane bilayer."	SDS	SP	A-6-26	-	A-1019-1039	disorder to order	papers	papers
P27958	1R7G	5978	set3	-	A	1978	1998	MemMoRF	intramembrane	15247283	-	"An α-helix extending from amino acid residue 5 to 25 was observed in the presence of different membrane mimetic media. This helix exhibited a hydrophobic, Trp rich side embedded in detergent micelles, while the polar, charged side was exposed to the solvent. Thus, the NS5A membrane anchor domain forms an in-plane amphipathic α-helix embedded in the cytosolic leaflet of the membrane bilayer."	DPC	SP	A-6-26	-	A-1019-1039	disorder to order	papers	papers
P27958	2KDR	16122	set1	-	X	1938	1965	MemMoRF	intracellular	19692468	-	"These results indicate a high propensity of NS4B[227–254] to interact with lipids and to adopt an α-helical structure upon lipid binding…. The amphipathic character, the positively charged residues, and the typical Trp interface residue (33), all of which are absolutely conserved among different HCV genotypes (Fig. 1A), suggest that the C-terminal half of the α-helix represents the main determinant for membrane association and likely interacts with the membrane interface in an in-plane topology, at least transiently."	TFE	MP	A-1-28	-	X-1054-1074	disorder to order	papers	papers
P28480	-	-	-	-	-	234	302	MemMoRF	intracellular	22988242	-	"CCT regulatory tails of diverse origins are composed of a long membrane lipid-inducible amphipathic helix (m-AH) followed by a highly disordered segment,"	-	-	-	-	-	disorder to order	papers	papers
P30273	-	-	-	-	-	62	81	MemMoRF	intracellular	19733547	-	"Here we analyzed membrane binding of intrinsically disordered ζcyt, CD3εcyt, and FcRγcyt, and found that there are two different modes of their lipid-binding activity toward acidic phospholipids (Figs. 3b and S2c): 1) coupled binding and folding that is characteristic for micelles and those vesicles that are unstable upon protein binding (DMPG), and 2) binding without folding that is observed in the presence of stable vesicles (POPG)."	POPG LUV, POPG SUV	SP	-	Disorder to order in LMPG micelles, DMPG SUV, DMPG LUV and disorder to disorder in POPG LUV, POPG SUV.	-	disorder to order	papers	papers
P35169	1W1N	-	-	-	-	2465	2470	MemMoRF	intracellular	15772072	-	-	aqueous	-	A-27-33	-	-	disorder to disorder	calculations	papers
P35169	2KIO	16284	set1	-	-	2465	2470	MemMoRF	intracellular	20042596	-	"Binding studies with different lipids indicate that y1fatc interacts specifically with a membrane-mimetic environment but appears not to recognize a specific lipid headgroup. In both, the structures of oxidized and reduced micelle-bound y1fatc, residues Ile-2456 to Trp-2470 of the lipid-binding motif form a hydrophobic bulb that has a rim of charged residues."	DPC	-	A-27-33	-	-	disorder to disorder	calculations	papers
P35169	2KIT	16295	set1	-	-	2465	2470	MemMoRF	intracellular	20042596	-	"Binding studies with different lipids indicate that y1fatc interacts specifically with a membrane-mimetic environment but appears not to recognize a specific lipid headgroup. In both, the structures of oxidized and reduced micelle-bound y1fatc, residues Ile-2456 to Trp-2470 of the lipid-binding motif form a hydrophobic bulb that has a rim of charged residues."	DPC	-	A-27-33	-	-	disorder to disorder	calculations	papers
P37001	1MM4	5557	set1	-	A	26	43	ordered	intramembrane	12357033	-	"Although a precise positioning of the helix was not possible, it probably lies on the surface of the membrane, given its amphipathic nature"	DPC	-	A-2-19	-	-	bistable helix	none	papers, structures
P37001	1MM5	5557	set2	-	A	26	43	ordered	intramembrane	12357033	-	"Although a precise positioning of the helix was not possible, it probably lies on the surface of the membrane, given its amphipathic nature"	OG micelles	-	A-2-19	-	-	bistable helix	none	papers, structures
P37840	1XQ8	-	-	-	A	3	37	MemMoRF	extracellular	15615727	-	"As evidenced by a number of biophysical techniques, aS is predominantly a random coil in aqueous solution but has been shown to adopt secondary structure of mostly helical nature upon association with negatively charged SUV or detergent micelle surfaces (10, 12, 13, 17). In every case, the repeat region mediates lipid or detergent interactions, whereas the hydro-philic tail remains free in solution. In the presence of SUV the large majority of aS molecules exist vesicle-bound (10). Based on the backbone1H-1H NOE and secondary chemical shift pattern, helical secondary structure has been attributed to the entire repeat region in the micelle-bound state with the excep-tion of a short stretch near Ser42-Thr44(12, 18). When associ-ated with SUVs of 300–400 Å diameter, electron paramagnetic resonance (EPR) data were interpreted as evidence for an un-interrupted helix extending throughout the entire repeat re-gion (19)."	SDS micelle, 70% SDS, 30% DPC	-	A-3-37	-	-	disorder to order	DisProt	papers
P37840	1XQ8	-	-	-	A	45	92	MemMoRF	extracellular	15615727	-	"As evidenced by a number of biophysical techniques, aS is predominantly a random coil in aqueous solution but has been shown to adopt secondary structure of mostly helical nature upon association with negatively charged SUV or detergent micelle surfaces (10, 12, 13, 17). In every case, the repeat region mediates lipid or detergent interactions, whereas the hydro-philic tail remains free in solution. In the presence of SUV the large majority of aS molecules exist vesicle-bound (10). Based on the backbone1H-1H NOE and secondary chemical shift pattern, helical secondary structure has been attributed to the entire repeat region in the micelle-bound state with the excep-tion of a short stretch near Ser42-Thr44(12, 18). When associ-ated with SUVs of 300–400 Å diameter, electron paramagnetic resonance (EPR) data were interpreted as evidence for an un-interrupted helix extending throughout the entire repeat re-gion (19)."	SDS micelle, 70% SDS, 30% DPC	-	A-45-92	-	-	disorder to order	DisProt	papers
P46531	5KZO	30147	set1	-	A	1767	1769	MemMoRF	intracellular	28439555	-	"Within the cytosolic juxtamembrane domain of Notch, membrane surface association of the Leu-Trp-Phe1769 segment is interesting in light of its overlap with the Trp-Phe-Pro1770 motif, which is known to be essential for the binding of the RBPJ-associated molecule (RAM) domain to a transcriptional activation partner CSL. Our results suggest that the Trp-Phe-Pro1770 motif may normally be “tucked away” via membrane surface association, making it unavailable for interaction with CSL or other proteins until the entire NICD is released from the membrane by γ-secretase cleavage." ... "The reentrant loop in the C-terminal JMD was maintained throughout the simulations."	DHPC/DMPC_bicelle	SP	A-55-57	-	A-24-44	disorder to disorder	DisProt	papers
P51161	2MM3	19843	set1	-	A	-	-	ordered	intracellular	26613247	-	"The helical region is additionally thought to be a key determinant in the interactions of iLBPs with membranes [32, 33]. An important difference though is that, while in FABPs [26] and some of the reported CRBP structures [34, 35] the helical region shows a considerable disorder in the apo state, in human I‐BABP it is well defined in both the free [9] and the bound forms."	aqueous	-	-	-	-	bistable helix	none	papers
P54710	2MKV	19797	set1	-	A	5	14	MemMoRF	extracellular	24794573	-	"water-exposed regions (Pro10-Pro16 and the C-terminus) exhibiting enhanced mobility." ... "Beyond the helical regions, the backbone of extracellular Trp4, Tyr5 and Leu6 and cytoplasmic Lys55, Arg56, and Arg57 associate with the micelle-water interface."	SDS	SP	A-5-14	See Figure 1 in 24794573	A-29-46	disorder to disorder	calculations, papers	papers
P54710	2MKV	19797	set1	-	A	17	25	MemMoRF	extracellular	24794573	-	"Helix h2 is preceded by a short helical segment (h1) that spans residues Phe17-Arg25 and includes the FXYD signature motif (FYYD in FXYD2)"	SDS	SP	A-17-25	-	A-29-46	disorder to disorder	calculations	papers
P54710	2MKV	19797	set1	-	A	51	63	MemMoRF	intracellular	24794573	-	"water-exposed regions (Pro10-Pro16 and the C-terminus) exhibiting enhanced mobility." ... "Beyond the helical regions, the backbone of extracellular Trp4, Tyr5 and Leu6 and cytoplasmic Lys55, Arg56, and Arg57 associate with the micelle-water interface."	SDS	SP	A-51-63	See Figure 1 24794573	A-29-46	disorder to disorder	calculations, papers	papers
P55957	1ZY3	-	-	-	-	-	-	ordered	intracellular	16475813	-	"while the helices of apoptotic activator tBID are mostly parallel to the membrane surface. The NMR results for binding of tBID to the membrane were confirmed by site-directed spin labeling methods for EPR spectroscopy (28)."	DPC	-	-	No data available about the exact regions.	-	bistable helix	none	papers
P55957	2M5I	19054	set1	-	-	-	-	ordered	intracellular	24158446	-	"tBid adopts an extended structure in 1-palmitoyl-2-hydroxy-sn-glycero-3-[phospho-RAC-(1-glycerol)] (LPPG) micelles with its six helices including the BH3 domain interacting with the micelles."	LPPG	-	-	-	-	bistable helix	none	papers
P55957	-	-	-	-	-	-	-	ordered	intracellular	19670908	-	"Here we describe the interactions of full-length tBID with BCL-XL in aqueous solution." ... "Although full-length tBID already has a significant amount of α-helical secondary structure in its free state, the NMR and ITC data show that its three-dimensional conformation is stabilized by binding BCL-XL."	aqueous	-	-	-	-	bistable helix	none	papers
P60201	-	-	-	-	-	258	277	MemMoRF	intracellular	26561987	-	"Melittin is one of the most widely studied amphiphatic membrane-lytic peptides. In a crystalline state, this 26 amino acid peptide can form a helix structure in which residues 2–11 from an α-helix followed by a kink (residues 11–13), another less defined α-helix (residues 13–23), and a highly basic unstructured C-terminus.(43)" ... "Both melittin and the PLP peptide have basic residues near their C-terminus and can form amphipathic helices that interact with lipid membranes."	-	MP	-	-	-	disorder to order	papers	papers
P60484	1D5R	-	-	-	A,A	260	269	MemMoRF	intracellular	25461777	-	"The CBR3 loop (PTEN260–269) with its basic AAs (K260, K263, K266, K267 and K269) binds strongly to PS and PIPs, and its hydrophobic L265 sidechain snorkels into the hydrophobic membrane core"	-	-	A-254-263	MemMoRF is in a loop.	-	disorder to order	papers	papers
P61013	1FJK	4907	set1	-	A	2	16	MemMoRF	intracellular	14507721	-	-	organic solvent	SP	A-4-16	-	A-32-52	disorder to order	calculations	other species
P61013	1FJP	4907	set1	-	A	2	16	MemMoRF	intracellular	14507721	-	-	organic solvent	SP	A-4-16	-	A-32-52	disorder to order	calculations	other species
P61015	1N7L	-	-	-	A	1	16	MemMoRF	intracellular	14507721	-	"The helix of domain IA for the structure of monomeric PLB in trifluoroethanol spans residues 3–18, whereas in the chloroform/methanol mixture this helix spans residues 4–16. Under our experimental conditions, we found that domain IA spans residues 2–16 with Thr-17 at the beginning of the structured loop."	DPC	SP	A-3-17	-	A-33-53	disorder to order	papers	papers, structures
P61015	2KB7	-	-	-	A	1	16	MemMoRF	intracellular	19509339	-	"The N-terminal amphipathic helical domain Ia (residues 1-16) rests on the surface of the lipid membrane with the hydrophobic face of domain Ia embedded in the membrane bilayer interior." ... "The monomeric form of PLN exists in equilibrium between a dynamically disordered R state and a more restricted T state (7, 8) and has 3 structural domains (helix–loop–helix) and 4 dynamic domains: Ia (residues 1–16), loop (17–22), Ib (residues 23–30), and II (residues 31–52) (9). As measured by NMR (10, 11) and EPR spectroscopies (7, 8, 12, 13), the T state is predominant (≈84%) in both micelles and lipid bilayers (14)."	DPC	SP	A-1-16	-	-	disorder to order	papers	papers, structures
P61015	2LPF	18256	set1	-	A	1	16	MemMoRF	intracellular	23968132	-	"Hence, the structural ensemble of pS16-PLN suggests that phosphorylation at Ser16 dramatically alters the conformational fluctuations of PLN and destabilises the secondary structure elements." ... "We then repeated the analysis for pS16-PLN. Our analysis indicates that phosphorylation at Ser16 induces a redistribution of the Boltzmann weights of the four states of PLN (Fig. 5). We found that the T state of pS16-PLN has a decreased population (37%) with respect to the unphosphorylated form (55%), and that the R′ and R states significantly increase in population (from 7% to 13% and from 4% to 12%, respectively). The result that the R state trebles its population upon phosphorylation is consistent with previous NMR34 and EPR36 results. Also, the increase in the population of the excited state is directly correlated to the loss of inhibitory function upon phosphorylation34, 36, 44. The reduction in the number of contacts for the R state is more pronounced for pS16-PLN, indicating a higher tendency of the N-terminal region to detach from the micelle surface (Fig. 6). This finding could arise from charge repulsion introduced upon phosphorylation."	DPC	SP	A-2-17	-	A-33-53	disorder to order	papers	papers, structures
P63045	2KOG	-	-	-	A	36	54	MemMoRF	intracellular	19918058	-	"The N-terminal SNARE motif helix is induced by the presence of the lipid micelle because it is unstructured in the absence of lipids, confirming previous results" ... "A second important structural feature is a nascent α-helix at the transition from the SNARE motif to the 10-residue juxtamembrane domain (residues 85–94) that links the SNARE motif (residues 28–84) with the TM domain (residues 95–116). Even before forming a complex with cognate SNAREs, this segment adopts a helical structure in its DPC-bound prefusion form" ... "Motions on the ps-ns time-scale, as well as amide hydrogen-exchange on the 10 ms time-scale provide strong evidence that helix I, but not helix II interacts with the micelle surface."	-	SP	A-39-57	-	A-98-117	disorder to order	DisProt, MFIB, papers	papers
P63045	2KOG	-	-	-	A	77	88	MemMoRF	intracellular	19918058	-	"Motions on the ps-ns time-scale, as well as amide hydrogen-exchange on the 10 ms time-scale provide strong evidence that helix I, but not helix II interacts with the micelle surface."	-	SP	A-80-91	-	A-98-117	disorder to order	DisProt, papers	papers, DisProt
P69428	2MN6	19714	set1	-	A,B	22	44	MemMoRF	intracellular	25090434	-	-	DPC	SP	A-25-44;B-25-44	-	B-4-24;A-4-24	disorder to order	DisProt, calculations	calculations, papers
P69428	2MN7	-	-	-	-	22	44	MemMoRF	intracellular	25090434	-	-	DPC	SP	-	-	A-1-21	disorder to order	DisProt, calculations	calculations, papers
P69428	-	-	-	-	A	22	44	MemMoRF	intracellular	12427031	-	"An expressed construct without the transmembrane segment is largely unstructured in aqueous solution but is able to insert into phospholipid monolayers and interacts with membrane bilayers. Protease accessibility experiments indicate that the extramembranous region of TatA is located at the cytoplasmic face of the cell membrane."	40 mg/mL solution of E. coli total membrane polar lipids (Avanti Polar Lipids) containing 1% (v/v) C12E9	SP	-	-	-	disorder to order	DisProt, calculations	calculations, papers
P69428	-	-	-	-	A	22	44	MemMoRF	intracellular	21683683	-	"NMR and CD spectroscopy of TatAH2 show that it adopts a predominantly helical structure in a membrane environment while remaining unstructured in aqueous solution. Differential scanning calorimetry studies also reveal that TatAH2 interacts with DPPG lipids but not with DPPC, suggesting that negatively charged phospholipid head groups contribute to the membrane interactions with TatA."	DPPG / DPPC	SP	-	-	-	disorder to order	DisProt, calculations	calculations, papers
P69539	1FDM	-	-	-	A	31	40	ordered	extracellular	9237913	-	"As shown in Figure 9, one of the families (A) presents a more favorable situation allowing the hydrophobic residues of the amphipathic helix to interact with the micelle and by correspondence with the surface of bilayers. The structures in family B were more similar than those in family A to the arrangement proposed by Papavoine et al. (1995) based on the effects of electron spin labels in the detergent molecules of the micelles on the relaxation properties of protein resonances."	SDS	SP	A-8-17	-	A-22-42	bistable helix	none	papers
P69539	1MZT	-	-	-	A	31	40	ordered	extracellular	12592011	-	"The 16‐Å‐long IP helix (residues 8–18) is amphipathic and rests on the membrane surface, with the boundary separating the polar and apolar residues parallel to the lipid bilayer surface, and the apolar residues facing the hydrocarbon core of the lipid bilayer (Fig. 3C)." ... "The resulting structure, shown in Figure 3, is particularly appealing because the dihedral angles of the connecting turn do not disrupt the sense of helix winding as the protein structure makes the transition from the N‐terminal IP helix to the C‐terminal TM helix. This is suggestive of a helix‐wind‐up conformational change during the phage assembly process, whereby tightening the winding around the connecting turn forces the IP helix to tilt up and to form the single, continuous, long α‐helix observed in the phage‐bound protein structure (Opella et al. 1987; Glucksman et al. 1992; Marvin et al. 1994)."	POPC/POPG	SP	A-8-17	-	A-22-42	bistable helix	none	papers
P69541	2CPB	-	-	-	A	32	40	ordered	extracellular	9735296	-	"the helix can now be defined more precisely: it comprises residues 8 to 16. This helix was found to be located at the surface of the micelle (Papavoine et al., 1994) showing considerable motional freedom on the nanosecond and picosecond time-scale" ... "Superposition of the different low-energy conformers (Figure 3(b)) shows that the hinge region (residues 17 to 24) has a structure that resembles an α-helix" ... "The latter residues (8, 12 and 15) are also important in the micellar system and show interactions with the micellar molecules Papavoine et al 1994, Papavoine et al 1995. The high-resolution structure of gVIIIp in SDS and DodPCho micelles has been determined. The structure consists of two well defined α-helices. A small amphipathic helix running from residues 8 to 16 and a longer hydrophobic helix from residues 25 to 45. The two helices are connected by a hinge region, which has a high α-helical content. The hinge region is less well defined than the two α-helices, probably as a result of protein mobility. This allows the amphipathic helix to move with respect to the hydrophobic helix. This mobility is on and away from the surface of the micelle, confirmed by results showing interactions between residues from the amphipathic helix and the detergent molecules. This interaction originates predominantly from the large side-chain molecules, which are located on one side of the amphipathic helix. The motion of the residues in the hinge region is the basis for the transition of the structural form of the gene-VIII protein in the membrane-bound form to that in the phage particle."	DPC	SP	A-9-17	-	A-25-45	bistable helix	none	papers
P69541	2CPS	4197	set1	-	A	32	40	ordered	extracellular	9735296	-	"the helix can now be defined more precisely: it comprises residues 8 to 16. This helix was found to be located at the surface of the micelle (Papavoine et al., 1994) showing considerable motional freedom on the nanosecond and picosecond time-scale" ... "Superposition of the different low-energy conformers (Figure 3(b)) shows that the hinge region (residues 17 to 24) has a structure that resembles an α-helix" ... "The latter residues (8, 12 and 15) are also important in the micellar system and show interactions with the micellar molecules Papavoine et al 1994, Papavoine et al 1995. The high-resolution structure of gVIIIp in SDS and DodPCho micelles has been determined. The structure consists of two well defined α-helices. A small amphipathic helix running from residues 8 to 16 and a longer hydrophobic helix from residues 25 to 45. The two helices are connected by a hinge region, which has a high α-helical content. The hinge region is less well defined than the two α-helices, probably as a result of protein mobility. This allows the amphipathic helix to move with respect to the hydrophobic helix. This mobility is on and away from the surface of the micelle, confirmed by results showing interactions between residues from the amphipathic helix and the detergent molecules. This interaction originates predominantly from the large side-chain molecules, which are located on one side of the amphipathic helix. The motion of the residues in the hinge region is the basis for the transition of the structural form of the gene-VIII protein in the membrane-bound form to that in the phage particle."	SDS	SP	A-9-17	-	A-25-45	bistable helix	none	papers
P70444	1DDB	-	-	-	-	147	192	ordered	intracellular	15501827	-	"Our data demonstrate that p15 BID upon targeting membranes partially unfolds and H6-H8 insert into the bilayer, yet maintaining an α-helical conformation. Most surprisingly, the helices do not adopt a transmembrane orientation but are parallel to the membrane surface with small tilting angles."	aqueous	-	-	-	-	bistable helix	none	papers
P78504	-	-	-	-	-	1087	1094	MemMoRF	intracellular	22465068	-	"J1C24 displays a marked helical propensity and undergoes a coil–helix transition in the presence of negatively charged, but not zwitterionic, lysophospholipid micelles. Phosphorylation at different positions drastically decreases the helical propensity of the peptides and abolishes the coil–helix transition triggered by lysophospholipid micelles. We propose that phosphorylation of residues upstream of the PDZ binding motif may shift the equilibrium from an ordered, membrane-bound, interfacial form of Jagged-1 C-terminal region to a more disordered form" ... "A possible scenario consistent with the observed line widths, relaxation and solvent exchange data is given by the presence of regions that are partially or totally embedded in the micelle (h1, h2, and h3), regions that bind the surface of the micelle, probably in a dynamical way (h4), and other regions that do not significantly interact with the micelle and freely tumble in solution (the C-terminal PDZ binding motif)."	-	SP	-	-	-	disorder to order	DisProt	papers
P78504	-	-	-	-	-	1111	1120	MemMoRF	intracellular	22465068	-	"J1C24 displays a marked helical propensity and undergoes a coil–helix transition in the presence of negatively charged, but not zwitterionic, lysophospholipid micelles. Phosphorylation at different positions drastically decreases the helical propensity of the peptides and abolishes the coil–helix transition triggered by lysophospholipid micelles. We propose that phosphorylation of residues upstream of the PDZ binding motif may shift the equilibrium from an ordered, membrane-bound, interfacial form of Jagged-1 C-terminal region to a more disordered form" ... "A possible scenario consistent with the observed line widths, relaxation and solvent exchange data is given by the presence of regions that are partially or totally embedded in the micelle (h1, h2, and h3), regions that bind the surface of the micelle, probably in a dynamical way (h4), and other regions that do not significantly interact with the micelle and freely tumble in solution (the C-terminal PDZ binding motif)."	-	SP	-	-	-	disorder to order	DisProt	papers
P78504	-	-	-	-	-	1136	1149	MemMoRF	intracellular	22465068	-	"J1C24 displays a marked helical propensity and undergoes a coil–helix transition in the presence of negatively charged, but not zwitterionic, lysophospholipid micelles. Phosphorylation at different positions drastically decreases the helical propensity of the peptides and abolishes the coil–helix transition triggered by lysophospholipid micelles. We propose that phosphorylation of residues upstream of the PDZ binding motif may shift the equilibrium from an ordered, membrane-bound, interfacial form of Jagged-1 C-terminal region to a more disordered form" ... "A possible scenario consistent with the observed line widths, relaxation and solvent exchange data is given by the presence of regions that are partially or totally embedded in the micelle (h1, h2, and h3), regions that bind the surface of the micelle, probably in a dynamical way (h4), and other regions that do not significantly interact with the micelle and freely tumble in solution (the C-terminal PDZ binding motif)."	-	SP	-	-	-	disorder to order	DisProt	papers
P78504	-	-	-	-	-	1203	1213	MemMoRF	intracellular	22465068	-	"J1C24 displays a marked helical propensity and undergoes a coil–helix transition in the presence of negatively charged, but not zwitterionic, lysophospholipid micelles. Phosphorylation at different positions drastically decreases the helical propensity of the peptides and abolishes the coil–helix transition triggered by lysophospholipid micelles. We propose that phosphorylation of residues upstream of the PDZ binding motif may shift the equilibrium from an ordered, membrane-bound, interfacial form of Jagged-1 C-terminal region to a more disordered form" ... "A possible scenario consistent with the observed line widths, relaxation and solvent exchange data is given by the presence of regions that are partially or totally embedded in the micelle (h1, h2, and h3), regions that bind the surface of the micelle, probably in a dynamical way (h4), and other regions that do not significantly interact with the micelle and freely tumble in solution (the C-terminal PDZ binding motif)."	-	SP	-	-	-	disorder to order	DisProt	papers
Q02297-10	-	-	-	-	-	9	19	MemMoRF	intracellular	25944317	-	"In this study, we carried out structural characterization of recombinantly produced NRG1 type III N-terminal cytoplasmic domain (NRG1-III-Nct). The results strongly suggest an intrinsically disordered structure for NRG1-III-Nct. Metal binding by the cytoplasmic domain was verified by different techniques, and it is likely that metal and membrane binding are connected to partial folding of this domain." ... "The protein showed helical conformation with increasing TFE concentration (Fig. 3f). This result is a sign of possible protein folding upon binding to an interaction partner, such as a membrane surface or metal ions. TFE lowers the solvent dielectric constant, thereby providing membrane-like conditions in solution."	TFE	SP	-	-	-	disorder to order	DisProt	papers
Q02297-10	-	-	-	-	-	58	69	MemMoRF	intracellular	25944317	-	"In this study, we carried out structural characterization of recombinantly produced NRG1 type III N-terminal cytoplasmic domain (NRG1-III-Nct). The results strongly suggest an intrinsically disordered structure for NRG1-III-Nct. Metal binding by the cytoplasmic domain was verified by different techniques, and it is likely that metal and membrane binding are connected to partial folding of this domain." ... "The protein showed helical conformation with increasing TFE concentration (Fig. 3f). This result is a sign of possible protein folding upon binding to an interaction partner, such as a membrane surface or metal ions. TFE lowers the solvent dielectric constant, thereby providing membrane-like conditions in solution."	TFE	SP	-	-	-	disorder to order	DisProt	papers
Q03463	2KNU	16477	set1	-	-	317	327	MemMoRF	intracellular	19891955	-	"Circular Dichroism data indicate that the peptide exhibits a clear propensity to adopt a helical folding in different membrane mimicking media, such as mixtures of water with fluorinated alcohols and phospholipids, with a slight preference for negative charged bilayers." ... "Drawing a consensus from all the predictions, reported in Fig. 1A, the existence of three helical regions—H1, H2 and H3—could be hypothesized in the C-terminal domain of E1. H1 is the shortest and the most hydrophilic helix, whereas H2 and H3 are more hydrophobic and show the features of transmembrane helices. The helical wheel representations of the three helices (Fig. 1B) show that all of them are amphipathic" ... "cholesterol induces a conformational change in the peptide, independently on the lipid charge" ... "According to the qualitative analysis based on the bar-diagram, the refined structure can be described as two helical stretches, a short one spanning from Ala 319 to Met 323 and a second, longer helix from Thr 329 to Leu 338. Unfortunately the great number of overlapping signals in N-terminal part does not allow a better definition of this region, but the presence of a longer helical segment cannot be excluded as suggested from the difference between the measured Hα chemical shift and the random coils reported in Fig. 3B."	HFIP/water	SP	A-3-13	In HFIP/water, H1 is presented as a nascent helix.	-	disorder to order	calculations	papers
Q39871	-	-	-	-	-	1	8	MemMoRF	unknown	23325560	-	"the 11-mer motif was disordered in aqueous solution, but adopted an α-helix in SDS micelles. NMR diffusion measurements demonstrated that the 11-mer motif was associated with SDS micelles. Paramagnetic quenching NMR experiments further revealed the orientation of the 11-mer motif with respect to the mimetic membrane: the ordered N-terminal segment was inserted into the mimetic membrane, and the disordered C-terminal segment was exposed to water." ... "the 11‐mer motif was not deeply buried in the center of hydrophobic core of the micelle."	SDS	-	-	-	-	disorder to order	papers	papers
Q61009	5KTF	30137	set1	-	A	409	419	MemMoRF	extracellular	28162952	-	"We also identify juxtamembrane regions of the extracellular domain of SR-BI that may interact with the lipid surface to facilitate cholesterol transport functions of the receptor." ... "we also purified an SR-BI fragment (residues 405–445) lacking the hydrophobic transmembrane domain and examined it using NMR. Interestingly, no HSQC peaks were observed when SR-BI(405–445) was initially suspended in an aqueous solution. However, addition of increasing amounts of LPPG detergent resulted in the appearance of peaks (Figure 8D) that corresponded closely to many of the resonances for residues 405–445 observed in the SR-BI(405–475) spectrum (Figure S1). This important observation suggests that SR-BI(405–445) requires a hydrophobic environment to fold into its native structural conformation, thereby suggesting that this region harbors a potential membrane-interacting juxtamembrane domain."	LPPG	MP	A-7-17	-	A-39-59	disorder to order	papers	papers
Q61009	5KTF	30137	set1	-	A	427	435	MemMoRF	extracellular	28162952	-	"We also identify juxtamembrane regions of the extracellular domain of SR-BI that may interact with the lipid surface to facilitate cholesterol transport functions of the receptor." ... "we also purified an SR-BI fragment (residues 405–445) lacking the hydrophobic transmembrane domain and examined it using NMR. Interestingly, no HSQC peaks were observed when SR-BI(405–445) was initially suspended in an aqueous solution. However, addition of increasing amounts of LPPG detergent resulted in the appearance of peaks (Figure 8D) that corresponded closely to many of the resonances for residues 405–445 observed in the SR-BI(405–475) spectrum (Figure S1). This important observation suggests that SR-BI(405–445) requires a hydrophobic environment to fold into its native structural conformation, thereby suggesting that this region harbors a potential membrane-interacting juxtamembrane domain."	LPPG	MP	A-25-33	-	A-39-59	disorder to order	papers	papers
Q61097	2LPE	17045	set1	-	A	71	83	ordered	intracellular	23250398	-	"CC-SAM functioned as a membrane-binding module. By combining nuclear magnetic resonance spectroscopy and experiments in cultured cells, we found that membrane binding was mediated by helix α3 of the CC motif and that mutating residues in α3 abolished targeting of KSR-1 to the plasma membrane." ... "Residues 71 to 83 in helix α3 interacted most strongly with the micelle. In order for this to happen, the CC-SAM domain must change its overall conformation. First, helix α2 must disengage from helix α3 to allow helix α3 to interact with the membrane. Furthermore, helices α1 to α2 and helices α4 to α10 would need to have relatively weak interactions with helix α3."	solvent	-	A-50-62	-	-	bistable helix	none	papers
Q69422	2MKB	19765	set1	-	A	848	867	MemMoRF	intracellular	24741107	-	"In the case of the GBV-B NS2(113–137) peptide, the hydrophobic helix at residues 116 to 135 includes a short stretch of polar and negatively charged amino acids (GENG; aa 129 to 132), which is likely flexible because of the presence of two glycine residues (Fig. 7C). The overall hydrophobic nature of this helix likely explains its prediction as a TM segment (Fig. 1). However, the hydrophobicity together with the dispersion of charged residues in this peptide are compatible with its location in the NS2 cytosolic domain (Fig. 5B), in interaction with the membrane interface (S6) (Fig. 3D and 4H)."	TFE	MP	A-4-23	Uniprot: TMH, Reference: peripheral	A-3-23;A-721-741;A-809-829;A-834-854;A-878-898;A-939-959;A-1020-1040;A-2000-2020	disorder to order	calculations	papers
Q8GT36	2FFT	6926	set1	-	A	34	41	MemMoRF	intracellular	17176085	-	"The major structural features of TSP9 in SDS micelles include an N-terminal α-helix and a C-terminal helical turn. In addition, secondary chemical shifts and sequential dαN(i, i+2) and dαN(i, i+3) NOE connectivities observed for residues F28–D32 and G59–S62, suggest that these regions are at least partially ordered. The structured elements of TSP9 contain mainly hydrophobic residues. Thus their structures in SDS micelles are likely induced by the hydrophobic environment inside the micelles. Residues in other regions are disordered and remain so even in the presence of SDS micelles. Because SDS and DPC micelles have been serving as good membrane mimics, the disorder-to-order conformational transition of TSP9 upon association with micelles may have significant physiological relevance." ... "The observation of interactions between the unstructured regions of TSP9 and SDS micelles suggests that these disordered regions may play a role in modulating the membrane association of TSP9. Conceivably, the large number of lysines in these regions may facilitate the attachment of TSP9 to the negatively-charged membrane. Furthermore, the three phosphorylation sites (T46, T53 and T60) are also located in the unstructured region and make contacts with SDS micelles. Thus, it is reasonable to assume that phosphorylation of these sites will lower the membrane association affinity of TSP9."	SDS	-	A-15-22	-	-	disorder to order	DisProt	calculations, papers
Q8GT36	2FFT	6926	set1	-	A	54	78	MemMoRF	intracellular	17176085	-	"The major structural features of TSP9 in SDS micelles include an N-terminal α-helix and a C-terminal helical turn. In addition, secondary chemical shifts and sequential dαN(i, i+2) and dαN(i, i+3) NOE connectivities observed for residues F28–D32 and G59–S62, suggest that these regions are at least partially ordered. The structured elements of TSP9 contain mainly hydrophobic residues. Thus their structures in SDS micelles are likely induced by the hydrophobic environment inside the micelles. Residues in other regions are disordered and remain so even in the presence of SDS micelles. Because SDS and DPC micelles have been serving as good membrane mimics, the disorder-to-order conformational transition of TSP9 upon association with micelles may have significant physiological relevance." ... "The observation of interactions between the unstructured regions of TSP9 and SDS micelles suggests that these disordered regions may play a role in modulating the membrane association of TSP9. Conceivably, the large number of lysines in these regions may facilitate the attachment of TSP9 to the negatively-charged membrane. Furthermore, the three phosphorylation sites (T46, T53 and T60) are also located in the unstructured region and make contacts with SDS micelles. Thus, it is reasonable to assume that phosphorylation of these sites will lower the membrane association affinity of TSP9."	SDS	-	A-35-59	-	-	disorder to disorder	DisProt	calculations, papers
Q8GT36	2FFT	6926	set1	-	A	94	98	MemMoRF	intracellular	17176085	-	"The major structural features of TSP9 in SDS micelles include an N-terminal α-helix and a C-terminal helical turn. In addition, secondary chemical shifts and sequential dαN(i, i+2) and dαN(i, i+3) NOE connectivities observed for residues F28–D32 and G59–S62, suggest that these regions are at least partially ordered. The structured elements of TSP9 contain mainly hydrophobic residues. Thus their structures in SDS micelles are likely induced by the hydrophobic environment inside the micelles. Residues in other regions are disordered and remain so even in the presence of SDS micelles. Because SDS and DPC micelles have been serving as good membrane mimics, the disorder-to-order conformational transition of TSP9 upon association with micelles may have significant physiological relevance." ... "The observation of interactions between the unstructured regions of TSP9 and SDS micelles suggests that these disordered regions may play a role in modulating the membrane association of TSP9. Conceivably, the large number of lysines in these regions may facilitate the attachment of TSP9 to the negatively-charged membrane. Furthermore, the three phosphorylation sites (T46, T53 and T60) are also located in the unstructured region and make contacts with SDS micelles. Thus, it is reasonable to assume that phosphorylation of these sites will lower the membrane association affinity of TSP9."	SDS	-	A-75-79	-	-	disorder to order	DisProt	calculations, papers
Q8N6T3	-	-	-	-	-	192	231	MemMoRF	intracellular	15944734	-	"Site-directed mutagenesis, limited proteolysis and circular dichroism experiments suggest that the ALPS motif, which is unstructured in solution, inserts bulky hydrophobic residues between loosely packed lipids and forms an amphipathic helix on highly curved membranes." ... "In conclusion, the mapping experiments presented in Figure 3 demonstrate that the region of ArfGAP1 that binds to highly curved lipid membranes is a motif of about 40 aa (between aa 192 and 231)."	-	-	-	-	-	disorder to order	PFAM, papers	papers
Q92542	2N7Q	25817	set1	-	A	696	700	MemMoRF	intracellular	26776682	-	"A sequence containing residues V696-A700 from the C-terminal juxtamembrane region is lipid accessible (Fig. 5). This five-residue sequence contains hydrophobic residues. Its interaction with micelles suggests that this region may interact with cell membrane or interact with a hydrophobic region of other proteins, which may be important for γ -secretase complex function."	SDS	SP	A-41-45	-	A-15-35	disorder to disorder	calculations	papers
Q92542	2N7R	25818	set1	-	A	696	700	MemMoRF	intracellular	26776682	-	"A sequence containing residues V696-A700 from the C-terminal juxtamembrane region is lipid accessible (Fig. 5). This five-residue sequence contains hydrophobic residues. Its interaction with micelles suggests that this region may interact with cell membrane or interact with a hydrophobic region of other proteins, which may be important for γ -secretase complex function."	DPC	SP	A-41-45	-	A-15-35	disorder to disorder	calculations	papers
Q96AC1	2LGX	17827	set1	-	A	74	83	ordered	intracellular	22078565	-	"At lower lipid/protein ratio where line broadening is less, we were able to map a cluster of residues whose chemical shifts are perturbed by PIP2 including H40, K74, H76, W77, and K81 (Figure 4E)."	LUV (POPC, POPS, PIP2)	-	A-81-90	-	-	bistable helix	none	papers
Q96AC1	6U4N	30659	set1	entity1	A	74	83	ordered	intracellular	31590942	-	-	aqueous	-	A-81-90	-	-	bistable helix	none	papers
Q96BM0	2LOQ	18221	set1	-	A	39	49	MemMoRF	unknown	22609626	-	"The connecting loops between the transmembrane helices of FAM14B and second and third transmembrane helices of TMEM14C contain an amphiphilic helix, which lies roughly perpendicular to the preceding transmembrane helix." ... "we can assume that the helices are located close to the surface of the LMPG micelle."	LMPG	MP	A-48-58	MemMoRF is in between two disordered regions, only structure for this protein.	A-23-43;A-68-88;A-90-110	disorder to order	calculations	calculations, papers
Q99IB8	2KZQ	17011	set1	-	A	684	703	MemMoRF	intracellular	21147916	-	"These structural features, together with the clear propensity of the E2-SC peptide to adopt an α-helical structure upon binding to lipid-like molecules, suggest that the central amphipathic helix associates with the membrane interface, at least transiently, in an inplane topology. The C-terminal helix also appeared to be relatively amphiphilic," ... "it is located at the membrane interface, maybe in an in-plane topology."	TFE	SP	A-1-20	-	A-47-67;A-79-99;A-104-124;A-135-155;A-203-223;A-250-270;A-979-999;A-1127-1147;A-1150-1170;A-1172-1192;A-1203-1223;A-2330-2350	disorder to order	papers	papers
Q99IB8	2KZQ	17011	set1	-	A	706	714	MemMoRF	intracellular	21147916	-	"These structural features, together with the clear propensity of the E2-SC peptide to adopt an α-helical structure upon binding to lipid-like molecules, suggest that the central amphipathic helix associates with the membrane interface, at least transiently, in an inplane topology. The C-terminal helix also appeared to be relatively amphiphilic," ... "it is located at the membrane interface, maybe in an in-plane topology."	TFE	SP	A-23-31	-	A-47-67;A-79-99;A-104-124;A-135-155;A-203-223;A-250-270;A-979-999;A-1127-1147;A-1150-1170;A-1172-1192;A-1203-1223;A-2330-2350	disorder to order	papers	papers
Q9GUM7	-	-	-	-	-	110	136	MemMoRF	intracellular	28596722	-	"The CPX-1 CTD contains tandem lipid binding motifs – termed the C-terminal (CT) and amphipathic helix (AH) motifs – that together sense membrane curvature to preferentially bind highly curved membranes (Snead et al., 2014)." ... "The adjacent amphipathic region is intrinsically disordered in the free state and adopts helical structure only upon binding to highly curved membrane surfaces" ... "The AH motif is now observed to extend from residue 110 to residue 136, and adopts an amphipathic helix that is interrupted in the region surrounding residue Gly116."	DPC	-	-	There is a nascent helix (371-373) which haven't been investigated.	-	disorder to order	papers	papers
Q9GUM7	-	-	-	-	-	137	143	MemMoRF	intracellular	28596722	-	"The CPX-1 CTD contains tandem lipid binding motifs – termed the C-terminal (CT) and amphipathic helix (AH) motifs – that together sense membrane curvature to preferentially bind highly curved membranes (Snead et al., 2014)." ... "we conclude that the CT motif likely binds to micelles in a disordered conformation devoid of secondary structure."	DPC	-	-	-	-	disorder to disorder	papers	papers
Q9NR61	-	-	-	-	-	662	685	MemMoRF	intracellular	18435556	-	"a fragment spanning the intracellular region of human Delta-4 is intrinsically disordered in solution, yet at the same time, in response to changes in the physico-chemical environment, can form inter-convertible secondary structures through its plastic C-terminal region (P3)" ... "The mainly helical conformation of P3 in the presence of SDS may, on the other hand, be representative of the membrane-bound, uncomplexed form of Delta-4"	-	SP	-	-	-	disorder to order	DisProt	papers
Q9WMX2	2KWZ	16892	set1	-	A	873	878	MemMoRF	intracellular	21187906	-	"The first small helix (64–69), which includes the short hydrophobic stretch VILL might be located in the membrane interface, possibly in-plane of the membrane." ... "helices observed in TMS2 and TMS3 are not classical membrane anchoring TM helices, since they contain polar and charged residues. In addition, the TMS2 helix exhibits an amphipathic character suggesting that it could associate with the membrane interface, at least transiently. Based on physicochemical considerations, a transmembrane orientation of this helix is expected to be achieved only upon interaction with another complementary transmembrane segment neutralizing the polar and charged residues located in the hydrophobic core of the membrane. In this context, it is possible that the transmembrane association of TMS2 and TMS3 occurs in the translocon during NS2 biosynthesis. Alternatively, these TMS might be first released into the cytosol where they could interact at the membrane interface and then associate with the membrane to adopt their final transmembrane topology." ... "three transmembrane, mainly helical segments (TMS1: 4–23; TMS2: 27–49; and TMS3: 72–94), connected by a small cytosolic loop (aa 24–26) and by a luminal segment (aa 50–71) containing a short helix supposed to interact with the membrane interface."	TFE	P	A-4-9	MemMoRF is in between two disordered regions, only structure for this protein region.	A-14-34;A-61-81;A-790-810;A-938-958;A-961-981;A-983-1003;A-1014-1034;A-2122-2142	disorder to order	calculations	papers
Q9Y6G1	2LOO	18219	set1	-	A	6	19	ordered	intracellular	22609626	-	"For HIGD1A, HIGD1B, TMEM141 and TMEM14A, the first transmembrane helix was preceded by an amphiphilic N-terminal helix; this helix is presumably located at the micelle-water interface"	LMPG	MP	A-15-28	ST4, Uniprot TM regions are not correlate with the structure.	A-10-30;A-33-53;A-88-108	bistable helix	none	papers
Q9Y6G1	2LOP	18220	set1	-	A	6	19	ordered	intracellular	22609626	-	"For HIGD1A, HIGD1B, TMEM141 and TMEM14A, the first transmembrane helix was preceded by an amphiphilic N-terminal helix; this helix is presumably located at the micelle-water interface"	LMPG	MP	A-15-28	ST4, Uniprot TM regions are not correlate with the structure.	A-10-30;A-33-53;A-88-108	bistable helix	none	papers
Q9Y6I3	1INZ	4959	set1	-	A	1	18	MemMoRF	intracellular	11161217	-	"Many residues in site 1 showed large chemical shift changes, suggesting a large structural change upon phosphoinositide binding (Fig. 2A). Deletion of the entire site 1 region (NH2-terminal, 18 residues) resulted in a complete loss of PtdIns(4,5)P2binding (Fig. 2F). Of the positively charged residues within this region, only Arg8 was shown to be essential for binding (Fig. 2F). Results suggest that site 1, the NH2-terminal unstructured region, was necessary for binding and adopted a specific conformation upon binding to PtdIns(4,5)P2."	aqueous	-	-	-	-	disorder to order	papers	papers
Q9YDF8	2KYH	16957	set1	-	A	27	34	MemMoRF	intracellular	20851706	-	"The solution structure identified an additional α-helix in the KvAP VSD at the N-terminus, S0, which is also observed in the Kv1.2-Kv2.1 paddle chimera structure 10. This helix was not modeled in the KvAP VSD crystal structure, perhaps because of its flexibility across multiple time scales prevented significant electron density to be observed. S0 is roughly positioned between the intracellular ends of S1 and S2, and the mix of NOEs to water, hydrophilic and hydrophobic D7PC resonances establish its interfacial location. This helix is conserved among other VSDs" ... "The amphipathic nature of this helix and its position at the edge of the VSD structure suggest that it interacts with the interfacial region of the D7PC micelle" ... "The S0 helix is also highly mobile, consistent with its poor placement within the NMR ensemble" ... "Combined with high R1 and low hetNOE, this suggests that S0 exhibits mobility across multiple timescales, further supporting the hypothesis that S0 is dislodged in the absence of a membrane bilayer."	DHPC	MP	A-10-17	-	A-22-46;A-51-75;A-92-108;A-112-128;A-143-167;A-205-236	disorder to order	calculations, papers	papers
Q9YDF8	2KYH	16957	set2	-	A	27	34	MemMoRF	intracellular	20851706	-	"The solution structure identified an additional α-helix in the KvAP VSD at the N-terminus, S0, which is also observed in the Kv1.2-Kv2.1 paddle chimera structure 10. This helix was not modeled in the KvAP VSD crystal structure, perhaps because of its flexibility across multiple time scales prevented significant electron density to be observed. S0 is roughly positioned between the intracellular ends of S1 and S2, and the mix of NOEs to water, hydrophilic and hydrophobic D7PC resonances establish its interfacial location. This helix is conserved among other VSDs" ... "The amphipathic nature of this helix and its position at the edge of the VSD structure suggest that it interacts with the interfacial region of the D7PC micelle" ... "The S0 helix is also highly mobile, consistent with its poor placement within the NMR ensemble" ... "Combined with high R1 and low hetNOE, this suggests that S0 exhibits mobility across multiple timescales, further supporting the hypothesis that S0 is dislodged in the absence of a membrane bilayer."	DHPC	MP	A-10-17	-	A-22-46;A-51-75;A-92-108;A-112-128;A-143-167;A-205-236	disorder to order	calculations, papers	papers
A0A140GKJ0	5U1D	-	-	-	C	5	14	MemMoRF	intracellular	9109681	-	"ICP47 Is Mainly Unstructured in Aqueous Solution"	-	-	C-5-14;C-22-31	-	-	disorder to order	papers	papers
A0A140GKJ0	5U1D	-	-	-	C	22	31	MemMoRF	intracellular	9109681	-	"ICP47 Is Mainly Unstructured in Aqueous Solution"	-	-	C-5-14;C-22-31	-	-	disorder to order	papers	papers
A0A140GKJ0	5U1D	-	-	-	C	5	14	MemMoRF	intracellular	16835230	-	"Its active domain was mapped to residues 3–34 and shown to encode all functional properties of the full-length protein. The active domain of ICP47 was reconstituted into oriented phospholipid bilayers and studied by proton-decoupled 15N and 2H solid-state NMR spectroscopy. In phospholipid bilayers, the protein adopts a helix-loop-helix structure, where the average tilt angle of the helices relative to the membrane surface is 15° ( 7°). The alignment of both structured domains exhibits a mosaic spread of 10°. A flexible dynamic loop encompassing residues 17 and18 separates the two helices."	-	-	C-5-14;C-22-31	-	-	disorder to order	papers	papers
A0A140GKJ0	5U1D	-	-	-	C	22	31	MemMoRF	intracellular	16835230	-	"Its active domain was mapped to residues 3–34 and shown to encode all functional properties of the full-length protein. The active domain of ICP47 was reconstituted into oriented phospholipid bilayers and studied by proton-decoupled 15N and 2H solid-state NMR spectroscopy. In phospholipid bilayers, the protein adopts a helix-loop-helix structure, where the average tilt angle of the helices relative to the membrane surface is 15° ( 7°). The alignment of both structured domains exhibits a mosaic spread of 10°. A flexible dynamic loop encompassing residues 17 and18 separates the two helices."	-	-	C-5-14;C-22-31	-	-	disorder to order	papers	papers
P02686-5	-	-	-	-	-	83	94	MemMoRF	intracellular	18326633	-	"In aqueous solution, the classic 18.5 kDa isoform of MBP is primarily disordered, but has transient α-helices that are stabilized by membrane-mimetic conditions"	-	-	-	-	-	disorder to order	homology, papers	homology, papers
P02730	4YZF	-	-	-	A,B,C,D	369	381	MemMoRF	intracellular	31540709	-	"Our analyses reveal that the AE1 linker region should not be considered as a mere connector between the two main domains. Its C-terminal conserved region is involved in specific lipid contacts"	-	-	A-383-401;B-383-401;C-383-401;D-383-401;A-506-518;B-506-518;C-506-518;D-506-518;A-593-600;B-593-600;C-593-600;D-593-600;A-801-830;B-801-830;C-801-830;D-801-830;A-873-887;B-873-887;C-873-887;D-873-887	-	A-404-427;A-436-456;A-460-476;A-486-506;A-519-541;A-571-591;A-603-623;A-664-684;A-701-737;A-761-800;B-404-427;B-436-456;B-460-476;B-486-506;B-519-541;B-571-591;B-603-623;B-664-684;B-701-737;B-761-800;C-404-427;C-436-456;C-460-476;C-486-506;C-519-541;C-571-591;C-603-623;C-664-684;C-701-737;C-761-800;D-404-427;D-436-456;D-460-476;D-486-506;D-519-541;D-571-591;D-603-623;D-664-684;D-701-737;D-761-800	disorder to disorder	missing residues	papers
P02730	4YZF	-	-	-	A,B,C,D	383	401	ordered	intracellular	31540709	-	"Contact analysis between AE1 and the headgroups ofanionic lipids POPS and PIP2in the CG-MD simulationsof all conformers reveals specific sites of interactions withanionic lipids. These are located in the H1 helix (residues383–401), cytoplasmic loops between TM4, 5 (residues506–518), TM6, 7 (residues 593–600), TM12, and 13 (res-idues 801–830), and the C-terminal region (residues 873–887) "	-	-	A-383-401;B-383-401;C-383-401;D-383-401;A-506-518;B-506-518;C-506-518;D-506-518;A-593-600;B-593-600;C-593-600;D-593-600;A-801-830;B-801-830;C-801-830;D-801-830;A-873-887;B-873-887;C-873-887;D-873-887	-	A-404-427;A-436-456;A-460-476;A-486-506;A-519-541;A-571-591;A-603-623;A-664-684;A-701-737;A-761-800;B-404-427;B-436-456;B-460-476;B-486-506;B-519-541;B-571-591;B-603-623;B-664-684;B-701-737;B-761-800;C-404-427;C-436-456;C-460-476;C-486-506;C-519-541;C-571-591;C-603-623;C-664-684;C-701-737;C-761-800;D-404-427;D-436-456;D-460-476;D-486-506;D-519-541;D-571-591;D-603-623;D-664-684;D-701-737;D-761-800	bistable helix	papers	papers
P02730	4YZF	-	-	-	A,B,C,D	383	401	ordered	intracellular	30011272	-	"Additionally, in some of the simulations, some of the helicity of H1 is lost."	-	-	A-383-401;B-383-401;C-383-401;D-383-401;A-506-518;B-506-518;C-506-518;D-506-518;A-593-600;B-593-600;C-593-600;D-593-600;A-801-830;B-801-830;C-801-830;D-801-830;A-873-887;B-873-887;C-873-887;D-873-887	-	A-404-427;A-436-456;A-460-476;A-486-506;A-519-541;A-571-591;A-603-623;A-664-684;A-701-737;A-761-800;B-404-427;B-436-456;B-460-476;B-486-506;B-519-541;B-571-591;B-603-623;B-664-684;B-701-737;B-761-800;C-404-427;C-436-456;C-460-476;C-486-506;C-519-541;C-571-591;C-603-623;C-664-684;C-701-737;C-761-800;D-404-427;D-436-456;D-460-476;D-486-506;D-519-541;D-571-591;D-603-623;D-664-684;D-701-737;D-761-800	bistable helix	papers	papers
P02730	4YZF	-	-	-	A,B,C,D	506	518	ordered	intracellular	31540709	-	"Contact analysis between AE1 and the headgroups of anionic lipids POPS and PIP2 in the CG-MD simulations of all conformers reveals specific sites of interactions with anionic lipids. These are located in the H1 helix (residues 383–401), cytoplasmic loops between TM4, 5 (residues 506–518), TM6, 7 (residues 593–600), TM12, and 13 (residues 801–830), and the C-terminal region (residues 873–887) "	-	-	A-383-401;B-383-401;C-383-401;D-383-401;A-506-518;B-506-518;C-506-518;D-506-518;A-593-600;B-593-600;C-593-600;D-593-600;A-801-830;B-801-830;C-801-830;D-801-830;A-873-887;B-873-887;C-873-887;D-873-887	-	A-404-427;A-436-456;A-460-476;A-486-506;A-519-541;A-571-591;A-603-623;A-664-684;A-701-737;A-761-800;B-404-427;B-436-456;B-460-476;B-486-506;B-519-541;B-571-591;B-603-623;B-664-684;B-701-737;B-761-800;C-404-427;C-436-456;C-460-476;C-486-506;C-519-541;C-571-591;C-603-623;C-664-684;C-701-737;C-761-800;D-404-427;D-436-456;D-460-476;D-486-506;D-519-541;D-571-591;D-603-623;D-664-684;D-701-737;D-761-800	bistable helix	none	papers
P02730	4YZF	-	-	-	A,B,C,D	593	600	ordered	intracellular	31540709	-	"Contact analysis between AE1 and the headgroups of anionic lipids POPS and PIP2 in the CG-MD simulations of all conformers reveals specific sites of interactions with anionic lipids. These are located in the H1 helix (residues 383–401), cytoplasmic loops between TM4, 5 (residues 506–518), TM6, 7 (residues 593–600), TM12, and 13 (residues 801–830), and the C-terminal region (residues 873–887) "	-	-	A-383-401;B-383-401;C-383-401;D-383-401;A-506-518;B-506-518;C-506-518;D-506-518;A-593-600;B-593-600;C-593-600;D-593-600;A-801-830;B-801-830;C-801-830;D-801-830;A-873-887;B-873-887;C-873-887;D-873-887	-	A-404-427;A-436-456;A-460-476;A-486-506;A-519-541;A-571-591;A-603-623;A-664-684;A-701-737;A-761-800;B-404-427;B-436-456;B-460-476;B-486-506;B-519-541;B-571-591;B-603-623;B-664-684;B-701-737;B-761-800;C-404-427;C-436-456;C-460-476;C-486-506;C-519-541;C-571-591;C-603-623;C-664-684;C-701-737;C-761-800;D-404-427;D-436-456;D-460-476;D-486-506;D-519-541;D-571-591;D-603-623;D-664-684;D-701-737;D-761-800	bistable region	none	papers
P02730	4YZF	-	-	-	A,B,C,D	801	830	ordered	intracellular	31540709	-	"Contact analysis between AE1 and the headgroups of anionic lipids POPS and PIP2 in the CG-MD simulations of all conformers reveals specific sites of interactions with anionic lipids. These are located in the H1 helix (residues 383–401), cytoplasmic loops between TM4, 5 (residues 506–518), TM6, 7 (residues 593–600), TM12, and 13 (residues 801–830), and the C-terminal region (residues 873–887) "	-	-	A-383-401;B-383-401;C-383-401;D-383-401;A-506-518;B-506-518;C-506-518;D-506-518;A-593-600;B-593-600;C-593-600;D-593-600;A-801-830;B-801-830;C-801-830;D-801-830;A-873-887;B-873-887;C-873-887;D-873-887	-	A-404-427;A-436-456;A-460-476;A-486-506;A-519-541;A-571-591;A-603-623;A-664-684;A-701-737;A-761-800;B-404-427;B-436-456;B-460-476;B-486-506;B-519-541;B-571-591;B-603-623;B-664-684;B-701-737;B-761-800;C-404-427;C-436-456;C-460-476;C-486-506;C-519-541;C-571-591;C-603-623;C-664-684;C-701-737;C-761-800;D-404-427;D-436-456;D-460-476;D-486-506;D-519-541;D-571-591;D-603-623;D-664-684;D-701-737;D-761-800	bistable region	none	papers
P02730	4YZF	-	-	-	A,B,C,D	873	887	ordered	intracellular	31540709	-	"Contact analysis between AE1 and the headgroups of anionic lipids POPS and PIP2 in the CG-MD simulations of all conformers reveals specific sites of interactions with anionic lipids. These are located in the H1 helix (residues 383–401), cytoplasmic loops between TM4, 5 (residues 506–518), TM6, 7 (residues 593–600), TM12, and 13 (residues 801–830), and the C-terminal region (residues 873–887) "	-	-	A-383-401;B-383-401;C-383-401;D-383-401;A-506-518;B-506-518;C-506-518;D-506-518;A-593-600;B-593-600;C-593-600;D-593-600;A-801-830;B-801-830;C-801-830;D-801-830;A-873-887;B-873-887;C-873-887;D-873-887	-	A-404-427;A-436-456;A-460-476;A-486-506;A-519-541;A-571-591;A-603-623;A-664-684;A-701-737;A-761-800;B-404-427;B-436-456;B-460-476;B-486-506;B-519-541;B-571-591;B-603-623;B-664-684;B-701-737;B-761-800;C-404-427;C-436-456;C-460-476;C-486-506;C-519-541;C-571-591;C-603-623;C-664-684;C-701-737;C-761-800;D-404-427;D-436-456;D-460-476;D-486-506;D-519-541;D-571-591;D-603-623;D-664-684;D-701-737;D-761-800	bistable region	none	papers
P60058	5A6U	-	-	-	C	30	40	MemMoRF	intracellular	8942632	-	"In pure aqueous solution, the peptide is remarkably unfolded. Forming a stable complex with dodecylphosphocholine micelles, it acquires a well-defined α-helix−loop−α-helix secondary structure, with the first helix, highly amphipathic, lying at the micelle surface."	-	-	C-5-23;C-30-40	It has a regulatory role, somewhat similar to phospholamban and FXYD bitopic proteins.	A-9-28;A-52-71;A-93-113;A-120-140;A-148-168;A-216-236;A-264-284;A-330-350;A-396-416;A-421-437;B-11-31;C-40-61	disorder to order	papers	papers
P60058	5A6U	-	-	-	C	5	23	MemMoRF	intracellular	8942632	-	"In pure aqueous solution, the peptide is remarkably unfolded. Forming a stable complex with dodecylphosphocholine micelles, it acquires a well-defined α-helix−loop−α-helix secondary structure, with the first helix, highly amphipathic, lying at the micelle surface."	-	-	C-5-23;C-30-40	It has a regulatory role, somewhat similar to phospholamban and FXYD bitopic proteins.	A-9-28;A-52-71;A-93-113;A-120-140;A-148-168;A-216-236;A-264-284;A-330-350;A-396-416;A-421-437;B-11-31;C-40-61	disorder to order	papers	papers
P63010	2XA7	-	-	-	B	1	12	MemMoRF	intracellular	20603002	-	"There are three other regions of highly positive electrostatic potential on this surface in addition to the α subunit PtdIns4,5P2-binding site (Figure 5). The first is formed by basic residues from the N terminus of β2 (Lys5, Lys12, Lys26, Lys27, Lys29, Lys36)."	-	-	B-4-12	Visible in the structure, but without secondary strucutral elements and bound to the surface of the complex.	-	disorder to unknown	high b factor	papers
P84092	2XA7	-	-	-	C	223	229	MemMoRF	intracellular	20603002	-	"The second basic region (Lys330, Lys334, Lys350, Lys352, Lys354, Lys356, Lys365, Lys367, Lys368, Lys373) was identified as a putative PtdIns4,5P2-binding site (Collins et al., 2002; Rohde et al., 2002)."	-	-	C-223-229	-	-	disorder to unknown	missing residues, papers	papers
Q12483	1U5T	-	-	-	A	1	19	MemMoRF	intracellular	18539118	-	"a deletion of the basic N-terminal 24 residues (Δ1–24) of VPS22 (construct h)" ... "Deletion of the VPS22-H0 (construct h) significantly decreased the membrane binding to all PIPs tested. Deletion of VPS22- H0 had no apparent effect on binding to PC:PE liposomes"	-	-	-	-	-	disorder to unknown	missing residues, papers	papers
Q676U5	5ZYX	-	-	-	A	12	31	MemMoRF	intracellular	31145591	-	"the peptide adopts a random coil conformation in aqueous buffer but folds into an α helix in the presence of D8PG micelles."	-	-	A-1-20	-	-	disorder to order	papers	papers
Q8BH64	2QPT	-	-	-	A	1	18	MemMoRF	intracellular	24508342	-	"The N Terminus Can Insert into Membranes, but Is Not Essential for Membrane Binding and Oligomerization"	-	-	-	-	-	disorder to unknown	missing residues, papers	papers
Q9Q6P4	4O6C	-	-	-	A,B,C,D,E,F	951	955	MemMoRF	extracellular	24505133	-	"A 'greasy finger' loop on the connector subdomain forms a prominent part of the hydrophobic protrusion and is mobile, as it is disordered in the DEN2 NS1 structure."	-	-	A-185-189;B-185-189;C-185-189;D-185-189;E-185-189;F-185-189	-	-	disorder to order	papers, homology	papers
P29990	4O6B	-	-	-	A,B	935	939	MemMoRF	extracellular	24505133	-	"A 'greasy finger' loop on the connector subdomain forms a prominent part of the hydrophobic protrusion and is mobile, as it is disordered in the DEN2 NS1 structure."	-	-	A-184-188;B-184-188	-	-	disorder to order	missing residues, papers	papers
Q9Q6P4	4O6C	-	-	-	A,B,C,D,E,F	899	919	MemMoRF	extracellular	24505133	-	-	-	-	A-133-153;B-133-153;C-133-153;D-133-153;E-133-153;F-133-153	From DisProt: "Flexible region in the West Nile Virus NS1 protein, corresponds to a disordered loop which is also disordered in the DENV2 NS1 protein. Corresponds to an antigenic region containing a conserved hydrophobic WKxW motif"	-	disorder to unknown	missing residues, papers	papers
Q05776	4XIZ	-	-	-	A,B	60	74	MemMoRF	intracellular	30850607	-	"The crystal structures display a range of conformations for the Ω loop" ... "conformational changes within the Ω loop and the C-terminal helix are important role for efficient substrate capture and delivery."	-	-	A-60-74;B-60-74	"The Ω loop partially covers the substrate/lipid binding covity; thus this loop is inherently immersed into the bilayer."	-	disorder to order	conformational diversity, papers	papers
O60493	2MXC	-	-	-	A	94	107	MemMoRF	intracellular	29520003	-	"An additional helix connects PPII to α2 and is supported by close Gly94:Phe97, Gly94:Leu98, and Ala96:Arg99 distances. This helix (α*) is missing from the earlier PX structures10, but is functionally significant in that it positions exposed hydrophobic and basic side chains to form the membrane insertion loop (MIL) next to the β1–β2 hairpin loop."	-	-	A-105-118	2YPS: missing residues at 98-112	-	disorder to order	missing residues, papers	papers
P12823	1R6R	-	-	-	A,B	14	23	MemMoRF	intracellular	25412346	-	"Here, we found that pep14-23 binds to anionic phospholipids, acquiring α-helical conformation. We then established its tridimensional structure via nuclear magnetic resonance (NMR) spectroscopy"	-	-	A-14-23;B-14-23	-	-	disorder to order	papers	papers
P61012	4KYT	-	-	-	B,C	1	16	MemMoRF	intracellular	-	-	-	-	-	B-1-16;C-1-16	-	A-49-69;A-90-110;A-254-273;A-296-313;A-758-777;A-788-808;A-829-851;A-898-917;A-931-949;A-965-985;B-32-52;C-32-52	disorder to order	missing residues	homology
P59113	-	-	-	-	-	147	152	MemMoRF	intracellular	22235127	-	"both kindlin and talin have an unstructured loop inserted at the same position of their respective F1 domains. In kindlins, despite their variable lengths, these loops still share some conservedamino acids." ... "The F1 loop in kindlin is longer than that of talin and NMR analysis revealed no helical propensity in the kindlin-1 F1 loop, instead membrane binding is mediated by a stretch of lysines at the N terminus of the loop."	-	-	-	-	-	disorder to disorder	papers	papers
Q9BQL6	-	-	-	-	-	166	171	MemMoRF	intracellular	22235127	-	"both kindlin and talin have an unstructured loop inserted at the same position of their respective F1 domains. In kindlins, despite their variable lengths, these loops still share some conservedamino acids." ... "The F1 loop in kindlin is longer than that of talin and NMR analysis revealed no helical propensity in the kindlin-1 F1 loop, instead membrane binding is mediated by a stretch of lysines at the N terminus of the loop."	-	-	-	-	-	disorder to disorder	papers	papers
P29274	-	-	-	-	-	293	412	MemMoRF	intracellular	25692595	DOI: 10.1016/j.bpj.2014.12.036	"Our SRCD, SAXS, and NMR results support the previously predicted disordered and extended conformation of the A2A-ct in solution. Interestingly, certain negatively charged membrane-mimicking compounds induce a conformational change, making the C-terminus more helical"	-	-	-	-	-	disorder to order	papers	papers
P60880	-	-	-	-	-	81	94	MemMoRF	intracellular	30916996	https://doi.org/10.1096/fj.201802796R	"In general, the SNAP25 loop region is disordered in solution. Once the cysteine‐rich domain interacts with the membrane, the loop region is transformed from a random coil to an α‐helix, and the hydrophobic residues and the positively charged residues around the cysteine‐rich domain promote membrane association."	-	-	-	-	-	disorder to order	papers	papers
P10121	6N9B	-	-	-	A,B	195	207	MemMoRF	intracellular	21543314	-	"We show that the membrane-targeting sequence is highly dynamic in solution, independent of nucleotides and directly responds to the density of anionic phospholipids by a random coil-helix transition."	-	-	A-1-13;B-1-13	-	-	disorder to order	papers	papers
Q9D0J4	1KSG	-	-	-	-	1	14	MemMoRF	intracellular	26488653	-	"The combined data verify the requirement of the N-terminal amphipathic helix for membrane binding of Arl2/3 and their interaction with UNC119a." ... "Surprisingly, and in contrast to what was found for other Arf family members, a nucleotide-independent membrane interaction was detected for Arl2."	-	-	A-2-16	X-ray structure with GDP does not show the N-terminal helix	-	disorder to order	missing residues	papers
O00165	-	-	-	-	-	261	273	MemMoRF	intracellular	31400305	-	"Hematopoietic-substrate-1 associated protein X-1 (HAX-1) is intrinsically disordered." ... "HAX-1 associates with lipid membranes." ... "HAX-1 undergoes structural rearrangement upon binding lipid membranes." ... "Moreover, initial studies suggested that HAX-1 is a mitochondrial membrane protein with residues 261–273 in the C-terminal tail acting as a membrane anchor [1]." ... "We found that HAX-1 adopts partial folding upon binding to membranes and accentuated preference for negatively charged lipids. NMR experiments in lipid membranes show that upon binding, HAX-1 restricts the motion of the cytosolic region of monomeric PLN, shifting its conformational equilibrium."	-	-	-	-	-	disorder to order	papers	papers