Kishore, R and Raghothama, S and Balaram, P (1987) Cystine peptides: The intramolecular antiparallel \beta sheet conformation of a 20-membered cyclic peptide disulfide. In: Biopolymers, 26 (6). pp. 873-891.
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Abstract
A 20-membered cyclic peptide disulfide has been synthesized as a conformational model for disulfide loops of limited ring size. 1H-nmr studies at 270 MHz establish the presence of three intramolecular hydrogen bonds involving the Leu, Val, and methylamide NH groups in $CDCl_3$. Evidence for peptide aggregation in $CDCl_3$ is also presented. A structural transition involving loosening of the hydrogen bond formed by the Val NH group is observed upon the measured addition of $(CD_3)_2SO$ to $CDCl_3$. Hydrogen-bonding studies, together with unusually low field positions of the Cys(1) and Cys(6) C H resonances and high $J_{HNC.H}$ values provide support for an intramolecular antiparallel \beta-sheet conformation, facilitated by a chain reversal at the Aib-Ala segment. Extensive nuclear Overhauser effect studies provide compelling evidence for the proposed conformation and also establish a type I'\beta-turn at the Aib-Ala residues, the site of the chain reversal.
Item Type: | Journal Article |
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Publication: | Biopolymers |
Publisher: | John Wiley & Sons, Inc. |
Additional Information: | Copyright of this article belongs to John Wiley & Sons, Inc. |
Keywords: | cyclic peptide disulfide;conformational model;hydrogen bond |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit Division of Chemical Sciences > Sophisticated Instruments Facility (Continued as NMR Research Centre) |
Date Deposited: | 07 Mar 2008 |
Last Modified: | 19 Sep 2010 04:12 |
URI: | http://eprints.iisc.ac.in/id/eprint/319 |
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