Helices and other secondary structures of beta- and gamma-peptides

The principal secondary structural motifs adopted by peptides assembled from beta-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-CbetaCalpha-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 gamma-peptides is also given. (C) 2005 Wiley Periodicals, Inc.