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

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