Theoretical prediction of the basic helix types in α,β‐hybrid peptides

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 α,β‐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 β‐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 α,β‐hybrid peptides could be of great importance for a rational peptide and protein design. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 408–413, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com