Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase.
about
Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration.Characterization of deamidation of barstar using electrospray ionization quadrupole time-of-flight mass spectrometry, which stabilizes an equilibrium unfolding intermediate.Unfolding of a small protein proceeds via dry and wet globules and a solvated transition stateHow cooperative are protein folding and unfolding transitions?The effect of C-terminal helix on the stability of FF domain studied by molecular dynamics simulation
P2860
Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase.
description
2009 nî lūn-bûn
@nan
2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Revealing a concealed intermed ...... the SH3 domain of PI3 kinase.
@ast
Revealing a concealed intermed ...... the SH3 domain of PI3 kinase.
@en
type
label
Revealing a concealed intermed ...... the SH3 domain of PI3 kinase.
@ast
Revealing a concealed intermed ...... the SH3 domain of PI3 kinase.
@en
prefLabel
Revealing a concealed intermed ...... the SH3 domain of PI3 kinase.
@ast
Revealing a concealed intermed ...... the SH3 domain of PI3 kinase.
@en
P1476
Revealing a concealed intermed ...... the SH3 domain of PI3 kinase.
@en
P2093
Ajazul Hamid Wani
Jayant B Udgaonkar
P304
P356
10.1016/J.JMB.2009.01.060
P407
P577
2009-02-04T00:00:00Z