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-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.
Seebach
Dieter
D
Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule Zürich, Wolfgang-Pauli-Strasse 10, CH-8093 Zürich, Switzerland. seebach@org.chem
Hook
David F
DF
Glättli
Alice
A
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
D010455:Peptides; D012996:Solutions