title: Helices and other secondary structures of beta- and gamma-peptides.
abstract: 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-C(beta)-C(alpha)-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.
authors.affiliation: Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule Zürich, Wolfgang-Pauli-Strasse 10, CH-8093 Zürich, Switzerland. seebach@org.chem
authors.forename: Dieter
authors.initials: D
authors.lastname: Seebach
authors.forename: David F
authors.initials: DF
authors.lastname: Hook
authors.forename: Alice
authors.initials: A
authors.lastname: Glättli
mesh_terms: D020816:Amino Acid Motifs; D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D012996:Solutions / Q000737:chemistry
chemical_list: D010455:Peptides; D012996:Solutions