Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system.
about
Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.Quinary protein structure and the consequences of crowding in living cells: leaving the test-tube behind.DnaK-Dependent Accelerated Evolutionary Rate in Prokaryotes.A systems biology approach to optimising hosts for industrial protein production.Role of Proteome Physical Chemistry in Cell Behavior.Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles.Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions.
P2860
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P2860
Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system.
description
2012 nî lūn-bûn
@nan
2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հոտեմբերին 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
Protein folding rates and ther ...... th the Hsp70 chaperone system.
@ast
Protein folding rates and ther ...... th the Hsp70 chaperone system.
@en
type
label
Protein folding rates and ther ...... th the Hsp70 chaperone system.
@ast
Protein folding rates and ther ...... th the Hsp70 chaperone system.
@en
prefLabel
Protein folding rates and ther ...... th the Hsp70 chaperone system.
@ast
Protein folding rates and ther ...... th the Hsp70 chaperone system.
@en
P2093
P2860
P356
P1433
P1476
Protein folding rates and ther ...... th the Hsp70 chaperone system.
@en
P2093
Ashok Sekhar
Hon Nam Lam
Silvia Cavagnero
P2860
P304
P356
10.1002/PRO.2139
P577
2012-10-01T00:00:00Z