On Unsatisfied Hydrogen Bonds in the N-Terminal Subdomain of Villin Headpiece

被引：3

作者：

Brown, Jeffrey W. ^{[1
]}

Farelli, Jeremiah D. ^{[1
]}

McKnight, C. James ^{[1
]}

机构：

[1] Boston Univ, Sch Med, Dept Physiol & Biophys, Boston, MA 02118 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2011年 / 413卷 / 03期

基金：

美国国家卫生研究院;

关键词：

villin headpiece; NMR; X-ray crystallography; protein folding; hydrogen bond; F-ACTIN; DOMAIN;

D O I：

10.1016/j.jmb.2011.08.024

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Villin headpiece is a small autonomously folding protein that has emerged as a model system for understanding the fundamental tenets governing protein folding. In this communication, we employ NMR and X-ray crystallography to characterize a point mutant, H41F, which retains actin-binding activity, is more thermostable but, interestingly, does not exhibit the partially folded intermediate observed of either wild-type or other similar point mutants. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：543 / 547

页数：5

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