Folding analysis of the most complex Stevedore's protein knot
about
Protein knotting through concatenation significantly reduces folding stabilityEntropic stabilization of a deubiquitinase provides conformational plasticity and slow unfolding kinetics beneficial for functioning on the proteasomeThe exclusive effects of chaperonin on the behavior of proteins with 52 knot.Topologically knotted deubiquitinases exhibit unprecedented mechanostability to withstand the proteolysis by an AAA+ protease.
P2860
Folding analysis of the most complex Stevedore's protein knot
description
2016 nî lūn-bûn
@nan
2016 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի օգոստոսին 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
Folding analysis of the most complex Stevedore's protein knot
@ast
Folding analysis of the most complex Stevedore's protein knot
@en
type
label
Folding analysis of the most complex Stevedore's protein knot
@ast
Folding analysis of the most complex Stevedore's protein knot
@en
altLabel
Folding analysis of the most complex Stevedore’s protein knot
@en
prefLabel
Folding analysis of the most complex Stevedore's protein knot
@ast
Folding analysis of the most complex Stevedore's protein knot
@en
P2860
P3181
P356
P1433
P1476
Folding analysis of the most complex Stevedore's protein knot
@en
P2093
Szu-Yu Chen
P2860
P2888
P3181
P356
10.1038/SREP31514
P407
P577
2016-08-16T00:00:00Z
P6179
1049528823