The landscape of the prion protein's structural response to mutation revealed by principal component analysis of multiple NMR ensembles
about
Emergence and evolution of yeast prion and prion-like proteins.Reactivation of mutant p53: Constraints on mechanism highlighted by principal component analysis of the DNA binding domain.Distributions of experimental protein structures on coarse-grained free energy landscapes.Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2-α2 loop and α2-α3.Discerning evolutionary trends in post-translational modification and the effect of intrinsic disorder: Analysis of methylation, acetylation and ubiquitination sites in human proteins
P2860
The landscape of the prion protein's structural response to mutation revealed by principal component analysis of multiple NMR ensembles
description
2012 nî lūn-bûn
@nan
2012 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի օգոստոսին 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
The landscape of the prion pro ...... ysis of multiple NMR ensembles
@ast
The landscape of the prion pro ...... ysis of multiple NMR ensembles
@en
The landscape of the prion pro ...... ysis of multiple NMR ensembles
@nl
type
label
The landscape of the prion pro ...... ysis of multiple NMR ensembles
@ast
The landscape of the prion pro ...... ysis of multiple NMR ensembles
@en
The landscape of the prion pro ...... ysis of multiple NMR ensembles
@nl
prefLabel
The landscape of the prion pro ...... ysis of multiple NMR ensembles
@ast
The landscape of the prion pro ...... ysis of multiple NMR ensembles
@en
The landscape of the prion pro ...... ysis of multiple NMR ensembles
@nl
P2860
P1476
The landscape of the prion pro ...... ysis of multiple NMR ensembles
@en
P2093
Deena M A Gendoo
Paul M Harrison
P2860
P304
P356
10.1371/JOURNAL.PCBI.1002646
P577
2012-08-09T00:00:00Z