title: Reengineering a type II beta-turn as a potential helix nucleator. Part I. Crystal structure of Boc-Val-Pro-(D)Asp-Asp-Val-OMe monohydrate.
abstract: The crystal structure of Boc-Val1-Pro2-(D)Asp3-Asp4-Val5-OMe is described as a type II beta-turn reengineered into a potential helix nucleator. (D)Asp3 in the peptide is responsible for the configurationally guided LD chiral type II beta-turn centered at Pro2-(D)Asp3, as well as the partially developed LL chiral type I beta-turn centered at Asp4-Val5 by acceptance of a conformation nucleating H-bond from Val5NH to its carboxylic oxygen.
authors.affiliation: Department of Biophysics, University of Madras, India.
authors.forename: F
authors.initials: F
authors.lastname: Fabiola
authors.forename: V
authors.initials: V
authors.lastname: Pattabhi
authors.forename: E B
authors.initials: EB
authors.lastname: Raju
authors.forename: S
authors.initials: S
authors.lastname: Durani
mesh_terms: D003460:Crystallization; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D015202:Protein Engineering; D017433:Protein Structure, Secondary
chemical_list: D009842:Oligopeptides; C110468:tert-butoxycarbonyl-valyl-prolyl-aspartyl-aspartyl-valine methyl ester