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beta.-Turn conformation of N-acetyl-L-prolylglycyl-L-phenylalanine. Crystal structure and solution studies

Samir, K and Brahmachari, TN and Bhat, V and Sudhakar, M and Vijayan, RS and Rapaka, RS and Bhatnagar, V and Ananthanarayanan, S (1981) beta.-Turn conformation of N-acetyl-L-prolylglycyl-L-phenylalanine. Crystal structure and solution studies. In: Journal Of The American Chemical Society, 103 (7). pp. 1703-1708.

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Official URL: http://pubs.acs.org/doi/abs/10.1021/ja00397a020

Abstract

Pro-Gly segments in peptides and proteins are prone to adopt the 0-turn conformation. This paper reports experimental data for the presence of this conformation in a linear tripeptide N-acetyl-L-prolylglycyl-L-phenylalanineb oth in the solid state and in solution. X-ray diffraction data on the tripeptide crystal show that it exists in the type I1 0-turn conformation. CD and proton NMR data show that this conformation persists in trifluoroethanol and methanol solutions in equilibrium with the nonhydrogen-bonded structures. Isomerization around the acetyl-prolyl bond is seen to take place in dimethyl sulfoxide solutions of the tripeptide.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to American Chemical Society.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 29 Jul 2009 03:01
Last Modified: 19 Sep 2010 05:38
URI: http://eprints.iisc.ernet.in/id/eprint/21750

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