A Crystalline beta-Hairpin Peptide Nucleated by a Type I’ Aib-D-Ala beta-Turn: Evidence for Cross-Strand Aromatic Interactions

Aravinda, Subrayashastry and Shamala, Narayanaswamy and Rajkishore, Rai and Gopi, Hosahudya N and Balaram, Padmanabhan (2002) A Crystalline beta-Hairpin Peptide Nucleated by a Type I’ Aib-D-Ala beta-Turn: Evidence for Cross-Strand Aromatic Interactions. In: Angewandte Chemie International Edition, 41 (20). pp. 3863-3865.

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Abstract

Recent progress in the design of beta-hairpin peptides[1] and beta-sheet models has been based on the ability to nucleate reverse turns of the appropriate stereochemistry. D-Pro-Gly[2] and to a lesser extent Asn-Gly[3] segments have been shown to facilitate formation of type I’ and II’ beta-turns, which are most often found at the site of sharp polypeptide chain reversal, that is, beta-hairpins in proteins.[4, 5] The prime turns, I’ and II’, can exert differing influences on the relative twist of the antiparallel strands. The I’ turn has the sense of twist that matches the twisting of adjacent beta-strands in proteins. In contrast, the II’ turn results in a more planar arrangement with the hairpin flattening to a considerable degree.[4a,e] The D-Pro-Xxx segment can in principle adopt both II’ and I’ turn conformations as si (D-Pro) values of +30 deg. and –120 deg. are energetically favorable.[1a, 5]

Item Type:	Journal Article
Publication:	Angewandte Chemie International Edition
Publisher:	John Wiley & Sons, Inc
Additional Information:	Copyright for this article belongs to John Wiley & Sons, Inc
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit Division of Physical & Mathematical Sciences > Physics
Date Deposited:	25 Aug 2008
Last Modified:	19 Sep 2010 04:14
URI:	http://eprints.iisc.ac.in/id/eprint/1251

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