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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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 |
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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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