Investigation of an anomalously accelerating substitution in the folding of a prototypical two-state protein.
about
A comparison of the folding kinetics of a small, artificially selected DNA aptamer with those of equivalently simple naturally occurring proteins.Biophysics of protein evolution and evolutionary protein biophysicsInferring the rate-length law of protein foldingThe Kinetic Stability of a Full-Length Antibody Light Chain Dimer Determines whether Endoproteolysis Can Release Amyloidogenic Variable DomainsProtein unfolding rates correlate as strongly as folding rates with native structure.
P2860
Investigation of an anomalously accelerating substitution in the folding of a prototypical two-state protein.
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Investigation of an anomalousl ...... rototypical two-state protein.
@ast
Investigation of an anomalousl ...... rototypical two-state protein.
@en
Investigation of an anomalousl ...... rototypical two-state protein.
@nl
type
label
Investigation of an anomalousl ...... rototypical two-state protein.
@ast
Investigation of an anomalousl ...... rototypical two-state protein.
@en
Investigation of an anomalousl ...... rototypical two-state protein.
@nl
prefLabel
Investigation of an anomalousl ...... rototypical two-state protein.
@ast
Investigation of an anomalousl ...... rototypical two-state protein.
@en
Investigation of an anomalousl ...... rototypical two-state protein.
@nl
P2093
P2860
P1476
Investigation of an anomalousl ...... prototypical two-state protein
@en
P2093
Camille Lawrence
Jennifer Kuge
Kareem Ahmad
P2860
P304
P356
10.1016/J.JMB.2010.08.049
P407
P577
2010-09-15T00:00:00Z