High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States.
about
The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State.Solution NMR investigation of the response of the lactose repressor core domain dimer to hydrostatic pressure.Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
P2860
High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States.
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2016 nî lūn-bûn
@nan
2016 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի հոտեմբերին 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
High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States.
@ast
High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States.
@en
type
label
High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States.
@ast
High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States.
@en
prefLabel
High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States.
@ast
High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States.
@en
P2093
P356
P1476
High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States.
@en
P2093
Catherine A Royer
Ivan Peran
Natalie Stenzoski
Scott A McCallum
Soichiro Kitazawa
P304
15260-15266
P356
10.1021/JACS.6B09887
P407
P577
2016-10-26T00:00:00Z