X-Pro peptides. A theoretical study of the hydrogen bonded conformations of (a-aminoisobutyryl-L -prolyl)n sequences

Prasad, BV Venkatram and Balaram, P (1982) X-Pro peptides. A theoretical study of the hydrogen bonded conformations of (a-aminoisobutyryl-L -prolyl)n sequences. In: International Journal of Biological Macromolecules, 4 (2). pp. 99-102.

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Abstract

Intramolecularly hydrogen bonded conformations of (Aib-Pro)n sequences have been analysed theoretically. Both 4�1 (C10 and 3�1 (C7 hydrogen bonded regular structures are shown to be stereochemically feasible. Conformational energies for the helical structures have been estimated using classical potential energy methods. Both C10 and C7 conformations have very similar energies. Pyrrolidine ring puckering has a pronounced effect on the energies, and only Cγ-endo puckered Pro residues can be accommodated. The theoretical calculations using spectroscopic data suggest that the recently proposed novel 310 helical conformation for benzyloxycarbonyl(Aib-Pro)4-methyl ester is in solution, is indeed energetically and stereochemically favourable.

Item Type:	Journal Article
Publication:	International Journal of Biological Macromolecules
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Publisher.
Keywords:	Polypeptide; stereochemistry; proline; α-aminoisobutyryl peptides
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	15 Dec 2009 06:43
Last Modified:	19 Sep 2010 05:46
URI:	http://eprints.iisc.ac.in/id/eprint/23491

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