Cis peptide bonds in proteins:: Residues involved, their conformations, interactions and locations
Cis peptide bonds in proteins:: Residues involved, their conformations, interactions and locations
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DOI：
10.1006/jmbi.1999.3217
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发表时间：
1999-11-19
影响因子：
5.6
通讯作者：
Chakrabarti, P
中科院分区：
文献类型：
--
作者：
Pal, D;Chakrabarti, P
对来自Brookhaven protein Data Bank的一组非冗余蛋白结构进行了分析，以找出残基偏好、局部构象、氢键和其他涉及顺式肽键的稳定相互作用。这导致了顺式肽介导的转的重新分类，其平均几何参数已被评估。脯氨酸环的侧链和主链扭转角的相互依赖性解释了为什么顺式肽中的脯氨酸环具有向下折叠。对含有脯氨酸和非脯氨酸残基的顺式肽进行比较，发现它们在构象、在二级结构中的位置、与分子中心的关系以及残基的相对可及性方面存在差异。讨论了突变研究结果与蛋白质折叠过程中顺反异构化的相关性。(C) 1999学术出版社。
An analysis of a non-redundant set of protein structures from the Brookhaven Protein Data Bank has been carried out to find out the residue preference, local conformation, hydrogen bonding and other stabilizing interactions involving cis peptide bonds. This has led to a reclassification of turns mediated by cis peptides, and their average geometrical parameters have been evaluated. The interdependence of the side and main-chain torsion angles of proline rings provided an explanation why such rings in cis peptides are found to have the DOWN puckering. A comparison of cis peptides containing proline and non-proline residues show differences in conformation, location in the secondary structure and in relation to the centre of the molecule, and relative accessibilities of residues. Relevance of the results in mutation studies and the cis-trans isomerization during protein folding is discussed. (C) 1999 Academic Press.