The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding Equilibria
about
Conditionally disordered proteins: bringing the environment back into the fold.Data describing the solution structure of the WW3* domain from human Nedd4-1An integrated bioinformatics platform for investigating the human E3 ubiquitin ligase-substrate interaction network.Multiple WW domains of Nedd4-1 undergo conformational exchange that is quenched upon peptide binding.
P2860
The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding Equilibria
description
2016 nî lūn-bûn
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2016 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
name
The Nedd4-1 WW Domain Recogniz ...... Folding and Binding Equilibria
@ast
The Nedd4-1 WW Domain Recogniz ...... Folding and Binding Equilibria
@en
The Nedd4-1 WW Domain Recogniz ...... Folding and Binding Equilibria
@nl
type
label
The Nedd4-1 WW Domain Recogniz ...... Folding and Binding Equilibria
@ast
The Nedd4-1 WW Domain Recogniz ...... Folding and Binding Equilibria
@en
The Nedd4-1 WW Domain Recogniz ...... Folding and Binding Equilibria
@nl
prefLabel
The Nedd4-1 WW Domain Recogniz ...... Folding and Binding Equilibria
@ast
The Nedd4-1 WW Domain Recogniz ...... Folding and Binding Equilibria
@en
The Nedd4-1 WW Domain Recogniz ...... Folding and Binding Equilibria
@nl
P50
P3181
P1433
P1476
The Nedd4-1 WW Domain Recogniz ...... Folding and Binding Equilibria
@en
P2093
Karima Medini
Michael Schmitz
P304
P3181
P356
10.1021/ACS.BIOCHEM.5B01028
P407
P50
P577
2016-02-02T00:00:00Z