An analysis of the helix-to-strand transition between peptides with identical sequence.
about
The effect of long-range interactions on the secondary structure formation of proteinsMultiple stable conformations account for reversible concentration-dependent oligomerization and autoinhibition of a metamorphic metallopeptidaseChSeq: A database of chameleon sequences.Statistical analysis and molecular dynamics simulations of ambivalent α-helices.Improving protein secondary structure prediction based on short subsequences with local structure similarityEVA: large-scale analysis of secondary structure prediction.Shaping up the protein folding funnel by local interaction: lesson from a structure prediction study.Helical ambivalency induced by point mutations.Discordant and chameleon sequences: their distribution and implications for amyloidogenicity.Birth, life and death of nascent polypeptide chains.On the properties and sequence context of structurally ambivalent fragments in proteins.Aggregation of Chameleon Peptides: Implications of α-Helicity in Fibril FormationWhat determines the structure and stability of KFFE monomers, dimers, and protofibrils?Detecting hidden sequence propensity for amyloid fibril formation.Performance of secondary structure prediction methods on proteins containing structurally ambivalent sequence fragments.Examination of possible structural constraints of MHC-binding peptides by assessment of their native structure within their source proteins.Molecular dynamics study of an insertion/duplication mutant of bacteriophage T4 lysozyme reveals the nature of α→β transition in full protein context.
P2860
Q24646775-69F44310-06EA-42DF-A8B0-256B44E3B13FQ27694815-A62D6C10-AE0B-47B2-93B3-148315917EC4Q30374636-8F1D70C6-4005-42FA-8808-0794E4C4B8C3Q33721429-324E2841-11FC-4A0D-B6F8-021408D4629FQ33766762-0451FA05-7A14-48FC-9604-29B8D69F81CCQ34113376-047B682B-727F-4EE0-BEB8-C698826C3426Q34480062-431CFC79-CF76-4BB1-BE01-852648DBD2EDQ34723714-B58394F3-BEB7-4F7B-A9EF-06F0D110FCFBQ34724075-BE555817-3873-42C6-8776-F7BDA34187BBQ35089834-B83371A6-4052-4BE0-89CE-2997AE59D488Q36631429-1A2AF04E-DD34-4807-919D-ABC42F066687Q37075230-EA8434F9-2F81-4FDB-8EB5-87E4880FD530Q37277489-5EF1DD79-B42E-490A-A4DA-8DD7AAB9963DQ41882613-CF86E0B1-F5E8-43B3-B103-17921F19F95DQ46479217-4AFC958F-3CD5-489F-8AF4-E6122584A704Q47617870-13178AF1-3907-406D-9F47-AF20610E1100Q51061591-126C7D62-CD9A-4BE9-97DA-B7A2C7A905AD
P2860
An analysis of the helix-to-strand transition between peptides with identical sequence.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
@zh-hant
name
An analysis of the helix-to-strand transition between peptides with identical sequence.
@en
An analysis of the helix-to-strand transition between peptides with identical sequence.
@nl
type
label
An analysis of the helix-to-strand transition between peptides with identical sequence.
@en
An analysis of the helix-to-strand transition between peptides with identical sequence.
@nl
prefLabel
An analysis of the helix-to-strand transition between peptides with identical sequence.
@en
An analysis of the helix-to-strand transition between peptides with identical sequence.
@nl
P2093
P2860
P1433
P1476
An analysis of the helix-to-strand transition between peptides with identical sequence
@en
P2093
P2860
P304
P356
10.1002/1097-0134(20001101)41:2<248::AID-PROT90>3.0.CO;2-J
P407
P50
P577
2000-11-01T00:00:00Z