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A designed (3-hairpin peptide in crystals

Karle, IL and Awasthi, SK and Balaram, P (1996) A designed (3-hairpin peptide in crystals. In: Proc Natl Acad Sci Unit States Am, 93 (16). pp. 8189-8193.

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Official URL: http://www.pnas.org/content/93/16/8189.short

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.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to National Academy of Sciences.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 19 May 2010 06:10
Last Modified: 13 Apr 2011 06:32
URI: http://eprints.iisc.ernet.in/id/eprint/27915

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