关于 villin 头部结构域 N 端亚结构域中未满足的氢键。
On unsatisfied hydrogen bonds in the N-terminal subdomain of villin headpiece.
机构信息
Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118, USA.
出版信息
J Mol Biol. 2011 Oct 28;413(3):543-7. doi: 10.1016/j.jmb.2011.08.024. Epub 2011 Aug 31.
Abstract
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.
摘要
微丝结合蛋白头部是一种小型的自主折叠蛋白，它已成为理解控制蛋白质折叠基本原理的模型系统。在本通讯中，我们采用 NMR 和 X 射线晶体学来表征一个点突变体 H41F，该突变体保留了肌动蛋白结合活性，热稳定性更高，但有趣的是，它没有表现出野生型或其他类似点突变体观察到的部分折叠中间体。
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