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A Designed beta-Hairpin Peptide

Awasthi, Satish Kumar and Raghothama, S and Balaram, P (1995) A Designed beta-Hairpin Peptide. In: Biochemical and Biophysical Research Communications, 216 (1). pp. 375-381.

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A synthetic octapeptide, Boc-Leu-Val-Val-D-Pro-Gly-Leu-Val-Val-OMe (1) has been designed as a model for a beta-hairpin conformation. Circular dichroism spectra in various organic solvents reveal a single negative band at 214-217 nm consistent with beta-sheet structures. NMR studies in CDCl3 and C6D6 establish the solvent shielded nature of the Leu(1), Val(3), Leu(6) and Val (8) NH groups. Nuclear Overhauser effects are observed between Val(7) CalphaH and Val(2) (CalphaH) protons providing strong support for a beta-hairpin conformation. Several important diagnostic interresidue NOEs establish a Type II′ beta-turn conformation for the D-Pro-Gly segment and extended conformations for the amino and carboxyl terminal tripeptide arms. The high solubility of the beta-hairpin peptide in organic solvents holds promise for the development of models for three and four stranded beta-sheets.

Item Type: Journal Article
Publication: Biochemical and Biophysical Research Communications
Publisher: Academic Press
Additional Information: Copyright for this article belongs to Academic Press.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Division of Chemical Sciences > Sophisticated Instruments Facility (Continued as NMR Research Centre)
Date Deposited: 04 Nov 2004
Last Modified: 26 Feb 2019 08:49
URI: http://eprints.iisc.ac.in/id/eprint/2258

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