Multi-state proteins: approach allowing experimental determination of the formation order of structure elements in the green fluorescent protein.
about
Exploring the folding pathway of green fluorescent protein through disulfide engineering.Isoforms of green fluorescent protein differ from each other in solvent molecules 'trapped' inside this protein.Co-evolutionary constraints of globular proteins correlate with their folding rates.Predicting protein folding rate change upon point mutation using residue-level coevolutionary information.
P2860
Multi-state proteins: approach allowing experimental determination of the formation order of structure elements in the green fluorescent protein.
description
2012 nî lūn-bûn
@nan
2012 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի նոյեմբերին 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
Multi-state proteins: approach ...... the green fluorescent protein.
@ast
Multi-state proteins: approach ...... the green fluorescent protein.
@en
Multi-state proteins: approach ...... the green fluorescent protein.
@nl
type
label
Multi-state proteins: approach ...... the green fluorescent protein.
@ast
Multi-state proteins: approach ...... the green fluorescent protein.
@en
Multi-state proteins: approach ...... the green fluorescent protein.
@nl
prefLabel
Multi-state proteins: approach ...... the green fluorescent protein.
@ast
Multi-state proteins: approach ...... the green fluorescent protein.
@en
Multi-state proteins: approach ...... the green fluorescent protein.
@nl
P2860
P1433
P1476
Multi-state proteins: approach ...... the green fluorescent protein.
@en
P2093
Anatoly S Glukhov
Tatiana V Povarnitsyna
P2860
P304
P356
10.1371/JOURNAL.PONE.0048604
P407
P577
2012-11-14T00:00:00Z