Determination of ultrafast protein folding rates from loop formation dynamics.
about
Using massively parallel simulation and Markovian models to study protein folding: examining the dynamics of the villin headpieceHigh-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein.A microscopic view of miniprotein folding: enhanced folding efficiency through formation of an intermediate.Chemical, physical, and theoretical kinetics of an ultrafast folding protein.Kinetics of contact formation and end-to-end distance distributions of swollen disordered peptidesAn unlocking/relocking barrier in conformational fluctuations of villin headpiece subdomainExtremely slow intramolecular diffusion in unfolded protein LEffect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomainQuantitative comparison of villin headpiece subdomain simulations and triplet-triplet energy transfer experimentsChallenges in protein folding simulations: Timescale, representation, and analysisEffects of denaturants on the dynamics of loop formation in polypeptides.Making connections between ultrafast protein folding kinetics and molecular dynamics simulations.Folding free-energy landscape of villin headpiece subdomain from molecular dynamics simulationsSlow motions in the hydrophobic core of chicken villin headpiece subdomain and their contributions to configurational entropy and heat capacity from solid-state deuteron NMR measurements.Glassy dynamics of protein methyl groups revealed by deuteron NMR.Reconciling the solution and X-ray structures of the villin headpiece helical subdomain: molecular dynamics simulations and double mutant cycles reveal a stabilizing cation-pi interaction.Microsecond folding experiments and simulations: a match is made.Ab initio folding of proteins with all-atom discrete molecular dynamics.Slow motions in chicken villin headpiece subdomain probed by cross-correlated NMR relaxation of amide NH bonds in successive residuesUltrafast folding kinetics and cooperativity of villin headpiece in single-molecule force spectroscopy.Fluorescence-based characterization of non-fluorescent transient states of tryptophan - prospects for protein conformation and interaction studies.Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.Common structural transitions in explicit-solvent simulations of villin headpiece foldingEvidence for a partially structured state of the amylin monomerMeasuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories.Triplet-triplet energy transfer studies on conformational dynamics in peptides and a protein.The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone.Exploring the role of internal friction in the dynamics of unfolded proteins using simple polymer models.Hydrophobic core formation and dehydration in protein folding studied by generalized-ensemble simulations.Thermodynamics of loop formation in the denatured state of rhodopseudomonas palustris cytochrome c': scaling exponents and the reconciliation problem.Salt effects on hydrophobic-core formation in folding of a helical miniprotein studied by molecular dynamics simulations.Diffusive Dynamics of Contact Formation in Disordered Polypeptides.Fractional Viscosity Dependence of Reaction Kinetics in Glass-Forming Liquids.Global optimization and folding pathways of selected alpha-helical proteins.
P2860
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P2860
Determination of ultrafast protein folding rates from loop formation dynamics.
description
2005 nî lūn-bûn
@nan
2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Determination of ultrafast protein folding rates from loop formation dynamics.
@ast
Determination of ultrafast protein folding rates from loop formation dynamics.
@en
type
label
Determination of ultrafast protein folding rates from loop formation dynamics.
@ast
Determination of ultrafast protein folding rates from loop formation dynamics.
@en
prefLabel
Determination of ultrafast protein folding rates from loop formation dynamics.
@ast
Determination of ultrafast protein folding rates from loop formation dynamics.
@en
P2093
P1476
Determination of ultrafast protein folding rates from loop formation dynamics.
@en
P2093
James Hofrichter
Jan Kubelka
William A Eaton
P304
P356
10.1016/J.JMB.2005.01.057
P407
P577
2005-04-01T00:00:00Z