Theoretical prediction of the basic helix types in α,β-hybrid peptides
Theoretical prediction of the basic helix types in α,β-hybrid peptides
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DOI：
10.1002/bip.20493
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发表时间：
2006-01-01
期刊：
影响因子：
2.9
通讯作者：
Hofmann, Hans-Jorg
中科院分区：
文献类型：
--
作者：
Baldauf, Carsten;Guenther, Robert;Hofmann, Hans-Jorg
本研究以从头算分子轨道(MO)理论为基础，对新型折叠分子α、β-杂交肽的所有可能的螺旋折叠模式及其稳定性及其详细的分子结构进行了全面的综述。结果表明，骨架折叠具有相当大的内在潜力。与其他多肽折叠分子一样，混合或β-螺旋的代表在更多的无极介质中最稳定，而极性环境有利于螺旋，氢键只指向一个方向。理论结果证实了在这些杂交肽的第一次实验研究中发现的氢键模式。选择特殊的骨架替换模式，α、β杂交肽的二级结构潜力对合理的多肽和蛋白质设计具有重要意义。(C)2006年威利期刊公司。
This study provides a complete overview on all possible helical folding patterns, their stabilities, and their detailed molecular structure in the novel foldamer class of alpha,beta-hybrid peptides on the basis of ab initio molecular orbital (MO) theory. The results indicate a considerable intrinsic potential of backbone folding. As found for other peptide foldamers, representatives of mixed or beta-helices are most stable in more apolar media, whereas polar environments favor the helices with the hydrogen bonds pointing in only one direction. The theoretical results confirm the hydrogen-bonding patterns found in the first experimental studies on these hybrid peptides. Selecting special backbone substitution patterns, the secondary structure potential of the alpha,beta-hybrid peptides could be of great importance for a rational peptide and protein design. (c) 2006 Wiley Periodicals, Inc.