Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C' position of the C-capping box of alpha-helices.
about
A test of proposed rules for helix capping: Implications for protein designComputational Design of Thermostabilizing d -Amino Acid SubstitutionsA novel method reveals that solvent water favors polyproline II over beta-strand conformation in peptides and unfolded proteins: conditional hydrophobic accessible surface area (CHASA).Simulation of the folding equilibrium of alpha-helical peptides: a comparison of the generalized Born approximation with explicit solventEnthalpy of helix-coil transition: missing link in rationalizing the thermodynamics of helix-forming propensities of the amino acid residuesRole of backbone solvation in determining thermodynamic beta propensities of the amino acids.Refolding upon force quench and pathways of mechanical and thermal unfolding of ubiquitin.Amino acid intrinsic alpha-helical propensities III: positional dependence at several positions of C terminusSwitch from thermal to force-driven pathways of protein refolding.CAPS-DB: a structural classification of helix-capping motifs.The fusion activity of HIV-1 gp41 depends on interhelical interactions.Noncharged amino acid residues at the solvent-exposed positions in the middle and at the C terminus of the alpha-helix have the same helical propensity.Contribution of a single hydrogen bond between betaHis81 of MHC class II I-E(k) and the bound peptide to the pH-dependent thermal stability.New force replica exchange method and protein folding pathways probed by force-clamp technique.
P2860
Q27637826-A169DFCD-D8E6-4DAB-8133-5F9122FA60B5Q27674761-0035064E-4D6E-4654-864E-C99732F671C9Q31133660-8A8B1C52-E462-4C0E-A307-F723B7EC9DF6Q33713877-7E32FAB2-AB74-46AE-8970-E48E8B7B67E6Q33818377-37DC61A7-ACBD-42BD-BD1D-C0D95E28AB12Q34009075-C162DC1E-6D2B-403F-AB72-68F89AABF548Q35545521-604F57FC-AE00-4F1B-BA4B-2C7E458FF138Q36639218-6042582D-B779-4B9C-834B-D54E457ABEA7Q38846712-2F3DF289-B2F6-4CFA-910E-1FCB590C7A20Q39973633-AECD6D43-8760-4020-8EB8-65E1374B1E43Q40445874-4DA9AC7F-EBBB-4B5A-BD44-1EB359862F77Q43152693-A1E34D72-BC9E-4485-BC4F-087057F10549Q44735993-492F6198-C56E-425C-9D40-91EEA84E3568Q51894579-1C2798A8-EED3-4BB0-A3FA-7EBB070B5C94
P2860
Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C' position of the C-capping box of alpha-helices.
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Hydration of the peptide backb ...... -capping box of alpha-helices.
@ast
Hydration of the peptide backb ...... -capping box of alpha-helices.
@en
type
label
Hydration of the peptide backb ...... -capping box of alpha-helices.
@ast
Hydration of the peptide backb ...... -capping box of alpha-helices.
@en
prefLabel
Hydration of the peptide backb ...... -capping box of alpha-helices.
@ast
Hydration of the peptide backb ...... -capping box of alpha-helices.
@en
P2093
P2860
P356
P1476
Hydration of the peptide backb ...... -capping box of alpha-helices.
@en
P2093
G I Makhatadze
S T Thomas
V V Loladze
P2860
P304
10670-10675
P356
10.1073/PNAS.191381798
P407
P577
2001-09-04T00:00:00Z