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Conformational energy map of a dipeptide unit in relation to infrared and nuclear magnetic resonance data

Ramachandran, GN and Chandrasekaran, R (1971) Conformational energy map of a dipeptide unit in relation to infrared and nuclear magnetic resonance data. In: Biopolymers, 10 (5). pp. 935-939.

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Abstract

The variation of energy of the conformation of a dipeptide unit with the dihedral angles \phi and \psi is a fundamental aspect, which is of great importance to the study of protein structure. Good reviews are available dealing with the energy changes associated with the variation of different parameters such as bond lengths, bond angles, dihedral angles etc. Also recently, attempts have been made to obtain satifactory expression for hydrogen bond energy as a function of the parameters relating to it . Although various results of interest in relation to the conformation of polypeptides and proteins have been worked out from such theory, the theoretical results have not been dirertly tested in many cases in relation to available data from physicochemical studies on a dipeptide unit, or fragments of simple compounds which sufficiently approximate to it. The purpose of this prelimiiiary note is to point out the possibility of making such tests and to indicate some results which show reasonable agreement with data obtained from infrared arid NMR studies.

Item Type: Journal Article
Additional Information: The copyright belongs to John Wiley & Sons, Inc.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 13 Feb 2007
Last Modified: 19 Sep 2010 04:21
URI: http://eprints.iisc.ernet.in/id/eprint/4053

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