Microsecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapie.
about
Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase.Nanopore analysis reveals differences in structural stability of ovine PrP(C) proteins corresponding to scrapie susceptible (VRQ) and resistance (ARR) genotypes.Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.Microsecond folding dynamics of apomyoglobin at acidic pHThermodynamic characterization of the unfolding of the prion protein.A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein.Comparing equilibrium and kinetic protein unfolding using time-resolved electrospray-coupled ion mobility mass spectrometry.
P2860
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P2860
Microsecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapie.
description
2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Microsecond unfolding kinetics ...... tibility to classical scrapie.
@ast
Microsecond unfolding kinetics ...... tibility to classical scrapie.
@en
type
label
Microsecond unfolding kinetics ...... tibility to classical scrapie.
@ast
Microsecond unfolding kinetics ...... tibility to classical scrapie.
@en
prefLabel
Microsecond unfolding kinetics ...... tibility to classical scrapie.
@ast
Microsecond unfolding kinetics ...... tibility to classical scrapie.
@en
P2093
P2860
P1433
P1476
Microsecond unfolding kinetics ...... tibility to classical scrapie.
@en
P2093
Heinrich Roder
Kai-Chun Chen
William J Wedemeyer
P2860
P304
P356
10.1016/J.BPJ.2011.07.024
P407
P577
2011-09-01T00:00:00Z