Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration.
about
Connecting the kinetics and energy landscape of tRNA translocation on the ribosomeSelenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure.An introduction to critical points for biophysicists; observations of compositional heterogeneity in lipid membranesInsights into protein folding mechanisms from large scale analysis of mutational effects.Measuring internal friction of an ultrafast-folding proteinChemical, physical, and theoretical kinetics of an ultrafast folding protein.Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance.What can solid state NMR contribute to our understanding of protein folding?Folding of the Pit1 homeodomain near the speed limit.Protein folding studied by single-molecule FRET.Making connections between ultrafast protein folding kinetics and molecular dynamics simulations.Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.Barrierless evolution of structure during the submillisecond refolding reaction of a small protein.Dynamics of one-state downhill protein folding.Thermodynamics and kinetics of protein folding under confinementRuggedness in the folding landscape of protein L.Comparing a simple theoretical model for protein folding with all-atom molecular dynamics simulations.Ultrafast folding kinetics and cooperativity of villin headpiece in single-molecule force spectroscopy.Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.Measuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories.A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain.Reassessing the folding of the KIX domain: evidence for a two-state mechanism
P2860
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P2860
Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration.
description
2007 nî lūn-bûn
@nan
2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Relaxation rate for an ultrafa ...... ical denaturant concentration.
@ast
Relaxation rate for an ultrafa ...... ical denaturant concentration.
@en
Relaxation rate for an ultrafa ...... ical denaturant concentration.
@nl
type
label
Relaxation rate for an ultrafa ...... ical denaturant concentration.
@ast
Relaxation rate for an ultrafa ...... ical denaturant concentration.
@en
Relaxation rate for an ultrafa ...... ical denaturant concentration.
@nl
prefLabel
Relaxation rate for an ultrafa ...... ical denaturant concentration.
@ast
Relaxation rate for an ultrafa ...... ical denaturant concentration.
@en
Relaxation rate for an ultrafa ...... ical denaturant concentration.
@nl
P2093
P356
P1476
Relaxation rate for an ultrafa ...... ical denaturant concentration.
@en
P2093
James Hofrichter
Jan Kubelka
Troy Cellmer
William A Eaton
P304
14564-14565
P356
10.1021/JA0761939
P407
P50
P577
2007-11-06T00:00:00Z