Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
about
Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system.Mapping the conformation of a client protein through the Hsp70 functional cycle.How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions.Structure and topology around the cleavage site regulate post-translational cleavage of the HIV-1 gp160 signal peptide.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
Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
description
2012 nî lūn-bûn
@nan
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
2012年论文
@zh
2012年论文
@zh-cn
name
Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
@en
Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
@nl
type
label
Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
@en
Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
@nl
prefLabel
Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
@en
Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
@nl
P2093
P2860
P356
P1433
P1476
Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
@en
P2093
Ashok Sekhar
Hon Nam Lam
Jung Ho Lee
Margarita Santiago
Silvia Cavagnero
P2860
P304
P356
10.1002/PRO.2087
P577
2012-06-11T00:00:00Z