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Conformational restrictions of peptides via backbone modification: Solution and crystal-state analysis of Boc-L-Pro-DZPhe-Gly-NH2

Piazzesi, AM and Bardi, R and Crisma, M and Banora, GM and Toniolo, C and Chauhan, VS and Kaur, P and Uma, K and Balaram, P (1991) Conformational restrictions of peptides via backbone modification: Solution and crystal-state analysis of Boc-L-Pro-DZPhe-Gly-NH2. In: Gazzetta Chimica Italiana, 121 (1). pp. 1-7.

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Abstract

An N-alpha-protected model tripeptide amide containing, in the central position, an alpha,beta-dehydrophenylalanine (Z-configurational isomer), Boc-L-Pro-DELTA-Z-Phe-Gly-NH2 (Boc, tert-butyloxycarbonyl), has been synthesized by solution methods and fully characterized. IR absorption and H-1 NMR studies provided evidence for the occurrence of a significant population of a conformer containing two consecutive, intramolecularly H-bonded (type II-III') beta-bends in solution. However, an X-ray diffraction analysis clearly indicates that only the type-II beta-bend structure survives in the crystal state.

Item Type: Journal Article
Additional Information: Copy right of this article belongs to Society Chimica Italiana.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 27 Apr 2010 05:30
Last Modified: 19 Sep 2010 06:00
URI: http://eprints.iisc.ernet.in/id/eprint/27284

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