Entrapping unusual folding characteristics of the beta-Ala residues in a model peptide: Boc-beta-Ala-Aib-beta-Ala-NHCH3.

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

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Official URL: http://onlinelibrary.wiley.com/doi/10.1034/j.1399-...

Abstract

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.

Item Type: Article
Additional Information: Copyright of this article belongs to Wiley.
Uncontrolled Keywords: b-Ala peptides; folded structures; peptide design; unusual H-bond; X-ray diffraction analysis
Subjects: Q Science > QD Chemistry
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 04 Jan 2012 15:00
Last Modified: 08 Jan 2015 09:51
URI: http://crdd.osdd.net/open/id/eprint/311

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