利用二硫键交联来探究一种设计的四螺旋束蛋白的结构和柔韧性。
Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein.
作者信息
Regan L, Rockwell A, Wasserman Z, DeGrado W
机构信息
Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880, USA.
出版信息
Protein Sci. 1994 Dec;3(12):2419-27. doi: 10.1002/pro.5560031225.
Abstract
The introduction of disulfide crosslinks is a generally useful method by which to identify regions of a protein that are close together in space. Here we describe the use of disulfide crosslinks to investigate the structure and flexibility of a family of designed 4-helix bundle proteins. The results of these analyses lend support to our working model of the proteins' structure and suggest that the proteins have limited main-chain flexibility.
摘要
引入二硫键交联是一种普遍有用的方法，可用于确定蛋白质中在空间上彼此靠近的区域。在此，我们描述了利用二硫键交联来研究一类设计的四螺旋束蛋白的结构和柔韧性。这些分析结果支持了我们关于该蛋白质结构的工作模型，并表明这些蛋白质的主链柔韧性有限。
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