Making connections between ultrafast protein folding kinetics and molecular dynamics simulations.
about
When fast is better: protein folding fundamentals and mechanisms from ultrafast approachesProtein structure prediction: assembly of secondary structure elements by basin-hopping.Selenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure.Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Coarse-Grained Models for Protein-Cell Membrane Interactions.Protein structure prediction using global optimization by basin-hopping with NMR shift restraints.Spectroscopic studies of protein folding: linear and nonlinear methodsQuantitative comparison of villin headpiece subdomain simulations and triplet-triplet energy transfer experimentsLow folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulationMinimalist probes for studying protein dynamics: thioamide quenching of selectively excitable fluorescent amino acids.Native state conformational heterogeneity of HP35 revealed by time-resolved FRET.Simple few-state models reveal hidden complexity in protein folding.Protein folding kinetics and thermodynamics from atomistic simulationComparing a simple theoretical model for protein folding with all-atom molecular dynamics simulations.Measuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories.The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone.MSMBuilder2: Modeling Conformational Dynamics at the Picosecond to Millisecond Scale.Fisetin inhibits Listeria monocytogenes virulence by interfering with the oligomerization of listeriolysin O.Separability between overall and internal motion: a protein folding problem.Thermodynamic origin of α-helix stabilization by side-chain cross-links in a small protein.Enhancing pairwise state-transition weights: A new weighting scheme in simulated tempering that can minimize transition time between a pair of conformational states.Modeling Protein Folding Pathways
P2860
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P2860
Making connections between ultrafast protein folding kinetics and molecular dynamics simulations.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Making connections between ult ...... olecular dynamics simulations.
@ast
Making connections between ult ...... olecular dynamics simulations.
@en
Making connections between ult ...... olecular dynamics simulations.
@nl
type
label
Making connections between ult ...... olecular dynamics simulations.
@ast
Making connections between ult ...... olecular dynamics simulations.
@en
Making connections between ult ...... olecular dynamics simulations.
@nl
prefLabel
Making connections between ult ...... olecular dynamics simulations.
@ast
Making connections between ult ...... olecular dynamics simulations.
@en
Making connections between ult ...... olecular dynamics simulations.
@nl
P2093
P2860
P356
P1476
Making connections between ult ...... olecular dynamics simulations.
@en
P2093
Eric R Henry
James Hofrichter
Troy Cellmer
William A Eaton
P2860
P304
P356
10.1073/PNAS.1019552108
P407
P577
2011-03-24T00:00:00Z