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

JOURNAL OF MOLECULAR BIOLOGY

卷:413

Article

Brown, Jeffrey W.¹  Farelli, Jeremiah D.¹  McKnight, C. James¹ 

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

关键词: villin headpiece;    NMR;    X-ray crystallography;    protein folding;    hydrogen bond;   

DOI  :  10.1016/j.jmb.2011.08.024

来源: Elsevier

【 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.

【 授权许可】

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