The structural basis of urea-induced protein unfolding in β-catenin
about
Time-dependent X-ray diffraction studies on urea/hen egg white lysozyme complexes reveal structural changes that indicate onset of denaturationInfluence of chemical denaturants on the activity, fold and zinc status of anthrax lethal factor.Hydrogen bonds are a primary driving force for de novo protein folding.Structural analyses combined with small-angle X-ray scattering reveals that the retention of heme is critical for maintaining the structure of horseradish peroxidase under denaturing conditions.
P2860
The structural basis of urea-induced protein unfolding in β-catenin
description
2014 nî lūn-bûn
@nan
2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
The structural basis of urea-induced protein unfolding in β-catenin
@ast
The structural basis of urea-induced protein unfolding in β-catenin
@en
The structural basis of urea-induced protein unfolding in β-catenin
@nl
type
label
The structural basis of urea-induced protein unfolding in β-catenin
@ast
The structural basis of urea-induced protein unfolding in β-catenin
@en
The structural basis of urea-induced protein unfolding in β-catenin
@nl
prefLabel
The structural basis of urea-induced protein unfolding in β-catenin
@ast
The structural basis of urea-induced protein unfolding in β-catenin
@en
The structural basis of urea-induced protein unfolding in β-catenin
@nl
P2093
P2860
P50
P1476
The structural basis of urea-induced protein unfolding in β-catenin
@en
P2093
Chengyu Jiang
Fangkun Ning
Gongyi Zhang
Haolin Liu
Jennifer Kemp
Jianye Zang
Xiaoxue Yan
P2860
P304
P356
10.1107/S1399004714018094
P577
2014-10-16T00:00:00Z