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脯氨酸残基对蛋白质构象的影响。

Influence of proline residues on protein conformation.

作者信息

MacArthur M W, Thornton J M

机构信息

Department of Biochemistry and Molecular Biology, University College, London, U.K.

出版信息

J Mol Biol. 1991 Mar 20;218(2):397-412. doi: 10.1016/0022-2836(91)90721-h.

DOI:10.1016/0022-2836(91)90721-h
PMID:2010917
Abstract

To study the influence of proline residues on three-dimensional structure, an analysis has been made of all proline residues and their local conformations extracted from the Brookhaven Protein Data bank. We have considered the conformation of the proline itself, the relative occurrence of cis and trans peptides preceding proline residues, the influence of proline on the conformation of the preceding residue and the conformations of various proline patterns (Pro-Pro, Pro-X-Pro, etc.). The results highlight the unique role of proline in determining local conformation.

摘要

为研究脯氨酸残基对三维结构的影响,我们对从布鲁克海文蛋白质数据库中提取的所有脯氨酸残基及其局部构象进行了分析。我们考虑了脯氨酸本身的构象、脯氨酸残基之前顺式和反式肽的相对出现频率、脯氨酸对前一个残基构象的影响以及各种脯氨酸模式(脯氨酸-脯氨酸、脯氨酸-X-脯氨酸等)的构象。结果突出了脯氨酸在确定局部构象方面的独特作用。

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