扭曲平行β-折叠的构象及蛋白质结构中手性的起源
Conformations of twisted parallel beta-sheets and the origin of chirality in protein structures.
作者信息
Weatherford D W, Salemme F R
出版信息
Proc Natl Acad Sci U S A. 1979 Jan;76(1):19-23. doi: 10.1073/pnas.76.1.19.
Abstract
An analysis of the conformational properties of parallel beta-pleated sheets suggests that an important factor in the generation of beta-sheet twist is the preference for nonplanar peptide bond distortions that impart local left-handed helical character to polypeptide chains. It is demonstrated that the introduction of such chiral distortions, which result from the tetrahedral deformation of the peptide nitrogen atoms, naturally produces right-twisted beta-sheet structures with optimal hydrogen bond geometry.
摘要
对平行β折叠片层构象性质的分析表明，β折叠片层扭曲产生的一个重要因素是对非平面肽键扭曲的偏好，这种扭曲赋予多肽链局部左手螺旋特征。结果表明，由肽氮原子的四面体变形引起的这种手性扭曲的引入，自然会产生具有最佳氢键几何结构的右旋β折叠片层结构。
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本文引用的文献
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Configurations of Polypeptide Chains With Favored Orientations Around Single Bonds: Two New Pleated Sheets.围绕单键具有有利取向的多肽链构型：两种新的折叠片层。
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