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–Cβ–Cα–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
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