Journal
BIOPOLYMERS
Volume 84, Issue 4, Pages 408-413Publisher
WILEY
DOI: 10.1002/bip.20493
Keywords
peptide foldamers; alternate hybrid peptides; secondary structure formation; peptide helices; ab initio MO theory
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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.
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