Helices and other secondary structures of β‐ and γ‐peptides

Abstract

The principal secondary structural motifs adopted by peptides assembled from β‐amino acid units are discussed: the 14‐, 12‐, 10‐, 12/10‐, and 8‐helices, as well as the hairpin turn, extended structures, stacks, and sheets. Features that promote a particular folding propensity are outlined and illustrated by structures determined in solution (NMR) and in the solid‐state (x‐ray). The N–C β–C α–CO dihedral angles from molecular dynamics simulations, which are indicative of a particular secondary structure, are presented. A brief description of a helix and a turn of γ‐peptides is also given. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 23–37, 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