title: A designed beta-hairpin peptide in crystals.
abstract: Beta-hairpin structures have been crystallographically characterized only in very short acyclic peptides, in contrast to helices. The structure of the designed beta-hairpin, t-butoxycarbonyl-Leu-Val-Val-D-Pro-Gly-Leu-Val-Val-OMe in crystals is described. The two independent molecules of the octapeptide fold into almost ideal beta-hairpin conformations with the central D-Pro-Gly segment adopting a Type II' beta-turn conformation. The definitive characterization of a beta-hairpin has implications for de novo peptide and protein design, particularly for the development of three- and four-stranded beta-sheets.
authors.affiliation: Laboratory for the Structure of Matter, Naval Research Laboratory, Washington, DC 20375-5341, USA.
authors.forename: I L
authors.initials: IL
authors.lastname: Karle
authors.forename: S K
authors.initials: SK
authors.lastname: Awasthi
authors.forename: P
authors.initials: P
authors.lastname: Balaram
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides