The dominant folding route minimizes backbone distortion in SH3.
about
Constructing sequence-dependent protein models using coevolutionary information.Pierced Lasso Bundles are a new class of knot-like motifsKnowing one's place: a free-energy approach to pattern regulationGeometrical Frustration in Interleukin-33 Decouples the Dynamics of the Functional Element from the Folding Transition State EnsembleStructure of the human monomeric NEET protein MiNT and its role in regulating iron and reactive oxygen species in cancer cells.Revealing the global map of protein folding space by large-scale simulations.
P2860
The dominant folding route minimizes backbone distortion in SH3.
description
2012 nî lūn-bûn
@nan
2012 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի նոյեմբերին 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 dominant folding route minimizes backbone distortion in SH3.
@ast
The dominant folding route minimizes backbone distortion in SH3.
@en
type
label
The dominant folding route minimizes backbone distortion in SH3.
@ast
The dominant folding route minimizes backbone distortion in SH3.
@en
prefLabel
The dominant folding route minimizes backbone distortion in SH3.
@ast
The dominant folding route minimizes backbone distortion in SH3.
@en
P2860
P1476
The dominant folding route minimizes backbone distortion in SH3.
@en
P2093
Heiko Lammert
Jeffrey K Noel
P2860
P304
P356
10.1371/JOURNAL.PCBI.1002776
P50
P577
2012-11-15T00:00:00Z