title: Entrapping unusual folding characteristics of the beta-Ala residues in a model peptide: Boc-beta-Ala-Aib-beta-Ala-NHCH3.
creator: Thakur, A K
creator: Venugopalan, P
creator: Kishore, Raghuvansh
subject: QD Chemistry
description: Crystal structure analysis of a model peptide: Boc-beta-Ala-Aib-beta-Ala-NHCH3 (beta-Ala: 3-amino propionic acid; Aib: alpha-aminoisobutyric acid) revealed distinct conformational preferences for folded [phi approximately 136 degrees, mu approximately -62 degrees, psi approximately 100 degrees] and semifolded [phi approximately 83 degrees, mu approximately -177 degrees, psi approximately -117 degrees] structures of the N-and C-terminus beta-Ala residues, respectively. The overall folded conformation is stabilized by unusual Ni...H-Ni+1 and nonconventional C-H...O intramolecular hydrogen bonding interactions.
publisher: Wiley
date: 2000-07
type: Article
type: PeerReviewed
format: application/pdf
identifier: http://crdd.osdd.net/open/311/1/kishore2000.3.pdf
relation: http://onlinelibrary.wiley.com/doi/10.1034/j.1399-3011.2000.00737.x/abstract
identifier:   Thakur, A K and Venugopalan, P and Kishore, Raghuvansh  (2000) Entrapping unusual folding characteristics of the beta-Ala residues in a model peptide: Boc-beta-Ala-Aib-beta-Ala-NHCH3.  The journal of peptide research : official journal of the American Peptide Society, 56 (1).  pp. 55-8.  ISSN 1397-002X     
relation: http://crdd.osdd.net/open/311/