A Designed Three Stranded beta-Sheet Peptide as a Multiple beta-Hairpin Model

Das, Chittaranjan and Raghothama, S and Balaram, P (1998) A Designed Three Stranded beta-Sheet Peptide as a Multiple beta-Hairpin Model. In: Journal of the American Chemical Society, 120 (23). pp. 5812-5813.

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Abstract

Beta-Hairpins are important elements in protein structure,1 implicated in the nucleation of beta-sheets in protein folding.2 Multiple hairpin structures, in which successive strands are connected by very short loops (2-5 residues), are found in the trans-membrane beta-barrel structures formed by the bacterial porins.3 Considerable recent attention has been directed toward the synthesis of isolated beta-hairpins, stable in both aqueous and organic solvents.4 In most cases the central nucleating segment has a high propensity to form either type I’ or type II’ beta-turn structures, a feature that occurs widely in protein structures.1 The design of peptides that mimic folding patterns observed in proteins, from first principles, provides a rigorous test of our understanding of the factors that determine polypeptide stereochemistry.

Item Type:	Journal Article
Publication:	Journal of the American Chemical Society
Publisher:	American Chemical Society
Additional Information:	Copyright for this article belongs to American Chemical Society.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit Division of Chemical Sciences > Sophisticated Instruments Facility (Continued as NMR Research Centre)
Date Deposited:	04 Oct 2004
Last Modified:	19 Sep 2010 04:16
URI:	http://eprints.iisc.ac.in/id/eprint/2082

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