Secondary structure propensities in peptide folding simulations: a systematic comparison of molecular mechanics interaction schemes.
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DelPhi: a comprehensive suite for DelPhi software and associated resourcesMapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerizationβ-hairpin forms by rolling up from C-terminal: topological guidance of early folding dynamicsStructural consequences of ATP hydrolysis on the ABC transporter NBD dimer: molecular dynamics studies of HlyB.Molecular dynamics simulations of a new branched antimicrobial peptide: a comparison of force fields.Order through disorder: hyper-mobile C-terminal residues stabilize the folded state of a helical peptide. a molecular dynamics studyThe intrinsic conformational features of amino acids from a protein coil library and their applications in force field development.Direct observations of conformational distributions of intrinsically disordered p53 peptides using UV Raman and explicit solvent simulationsForce Field Benchmark of Organic Liquids: Density, Enthalpy of Vaporization, Heat Capacities, Surface Tension, Isothermal Compressibility, Volumetric Expansion Coefficient, and Dielectric Constant.Achieving secondary structural resolution in kinetic measurements of protein folding: a case study of the folding mechanism of Trp-cage.Molecular dynamics simulations of voltage-gated cation channels: insights on voltage-sensor domain function and modulation.Improving the description of salt bridge strength and geometry in a Generalized Born model.Inclusion of many-body effects in the additive CHARMM protein CMAP potential results in enhanced cooperativity of α-helix and β-hairpin formationUsing D-Amino Acids to Delineate the Mechanism of Protein Folding: Application to Trp-cage.Three force fields' views of the 3(10) helix.Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes.Effects of different force fields and temperatures on the structural character of Abeta (12-28) peptide in aqueous solution.Effect of intrinsic and extrinsic factors on the simulated D-band length of type I collagen.Intramolecular interactions stabilizing compact conformations of the intrinsically disordered kinase-inhibitor domain of Sic1: a molecular dynamics investigation.Interaction of β-sheet folds with a gold surface.Stability of transmembrane amyloid β-peptide and membrane integrity tested by molecular modeling of site-specific Aβ42 mutations.Structural dynamics of neuropeptide hPYY.Comparison of the structural characteristics of Cu(2+)-bound and unbound α-syn12 peptide obtained in simulations using different force fields.About the structural role of disulfide bridges in serum albumins: evidence from protein simulated unfolding.Effects of different force fields on the structural character of α synuclein β-hairpin peptide (35-56) in aqueous environment.
P2860
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P2860
Secondary structure propensities in peptide folding simulations: a systematic comparison of molecular mechanics interaction schemes.
description
2009 nî lūn-bûn
@nan
2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
name
Secondary structure propensiti ...... mechanics interaction schemes.
@ast
Secondary structure propensiti ...... mechanics interaction schemes.
@en
type
label
Secondary structure propensiti ...... mechanics interaction schemes.
@ast
Secondary structure propensiti ...... mechanics interaction schemes.
@en
prefLabel
Secondary structure propensiti ...... mechanics interaction schemes.
@ast
Secondary structure propensiti ...... mechanics interaction schemes.
@en
P2860
P1433
P1476
Secondary structure propensiti ...... mechanics interaction schemes.
@en
P2093
Bert L de Groot
P2860
P304
P356
10.1016/J.BPJ.2009.04.061
P407
P50
P577
2009-07-01T00:00:00Z