Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptide.

Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptide.

Item
http://www.wikidata.org/entity/Q31940101
Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solutionStructural characterization of a mutant peptide derived from ubiquitin: Implications for protein foldingFine grained sampling of residue characteristics using molecular dynamics simulation.Molecular Dynamics Simulations of 441 Two-Residue Peptides in Aqueous Solution: Conformational Preferences and Neighboring Residue Effects with the Amber ff99SB-ildn-NMR Force Field.The intrinsic conformational propensities of the 20 naturally occurring amino acids and reflection of these propensities in proteins.The intrinsic conformational features of amino acids from a protein coil library and their applications in force field development.Effects of turn residues in directing the formation of the beta-sheet and in the stability of the beta-sheet.Monomeric Aβ(1-40) and Aβ(1-42) Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil.On the properties and sequence context of structurally ambivalent fragments in proteins.A self-consistent description of the conformational behavior of chemically denatured proteins from NMR and small angle scattering.Overview of protein folding mechanisms: experimental and theoretical approaches to probing energy landscapes.Sequence-specific conformational flexibility of SNARE transmembrane helices probed by hydrogen/deuterium exchange.Reinvestigation of the proposed folding and self-association of the Neuropeptide Head Activator.Comparative analysis of amino acid sequences from envelope proteins isolated from different hepatitis C virus variants: possible role of conservative and variable regions.Expected and unexpected results from combined beta-hairpin design elements.Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins.Folding of a β-hairpin peptide derived from the N-terminus of ubiquitin
P2860

Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptide.

Item
http://www.wikidata.org/entity/Q31940101
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Modulation of intrinsic phi,ps ...... ion of a beta-hairpin peptide.
@ast
Modulation of intrinsic phi,ps ...... ion of a beta-hairpin peptide.
@en
type
label
Modulation of intrinsic phi,ps ...... ion of a beta-hairpin peptide.
@ast
Modulation of intrinsic phi,ps ...... ion of a beta-hairpin peptide.
@en
altLabel
Modulation of intrinsic φ,ψ pr ...... tide 1 1Edited by P. E. Wright
@en
prefLabel
Modulation of intrinsic phi,ps ...... ion of a beta-hairpin peptide.
@ast
Modulation of intrinsic phi,ps ...... ion of a beta-hairpin peptide.
@en
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P356
P1433
P1476
Modulation of intrinsic phi,ps ...... tion of a beta-hairpin peptide
@en
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698