Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion.
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Kinetic response of a photoperturbed allosteric proteinDefining a length scale for millisecond-timescale protein conformational exchange.Understanding the mechanism of proteasome 20S core particle gating.Molecular origins of internal friction effects on protein-folding rates.Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.Effect of viscogens on the kinetic response of a photoperturbed allosteric protein.An exact solution for R2,eff in CPMG experiments in the case of two site chemical exchangeCPMG Experiments for Protein Minor Conformer Structure Determination.
P2860
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P2860
Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion.
description
2012 nî lūn-bûn
@nan
2012 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Folding of the four-helix bund ...... predominantly by water motion.
@ast
Folding of the four-helix bund ...... predominantly by water motion.
@en
type
label
Folding of the four-helix bund ...... predominantly by water motion.
@ast
Folding of the four-helix bund ...... predominantly by water motion.
@en
prefLabel
Folding of the four-helix bund ...... predominantly by water motion.
@ast
Folding of the four-helix bund ...... predominantly by water motion.
@en
P2860
P356
P1476
Folding of the four-helix bund ...... predominantly by water motion.
@en
P2093
Ashok Sekhar
Pramodh Vallurupalli
P2860
P304
19268-19273
P356
10.1073/PNAS.1212036109
P407
P50
P577
2012-11-05T00:00:00Z