Subdomain interactions foster the design of two protein pairs with ∼80% sequence identity but different folds.
about
The role of negative selection in protein evolution revealed through the energetics of the native state ensemble.Studying protein fold evolution with hybrids of differently folded homologsStructural origins of misfolding propensity in the platelet adhesive von Willebrand factor A1 domain.Two is a pair, three is a network.Multisequence algorithm for coarse-grained biomolecular simulations: Exploring the sequence-structure relationship of proteins.Extant fold-switching proteins are widespread.
P2860
Subdomain interactions foster the design of two protein pairs with ∼80% sequence identity but different folds.
description
2015 nî lūn-bûn
@nan
2015 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Subdomain interactions foster ...... identity but different folds.
@ast
Subdomain interactions foster ...... identity but different folds.
@en
Subdomain interactions foster ...... identity but different folds.
@nl
type
label
Subdomain interactions foster ...... identity but different folds.
@ast
Subdomain interactions foster ...... identity but different folds.
@en
Subdomain interactions foster ...... identity but different folds.
@nl
prefLabel
Subdomain interactions foster ...... identity but different folds.
@ast
Subdomain interactions foster ...... identity but different folds.
@en
Subdomain interactions foster ...... identity but different folds.
@nl
P2093
P2860
P1433
P1476
Subdomain interactions foster ...... e identity but different folds
@en
P2093
John Orban
Philip N Bryan
Yihong Chen
P2860
P304
P356
10.1016/J.BPJ.2014.10.073
P407
P577
2015-01-01T00:00:00Z