Conformational study of valinomycin: a molecular dynamics approach

Shobana, S and Vishveshwara, Saraswathi (1996) Conformational study of valinomycin: a molecular dynamics approach. In: Biophysical Chemistry, 57 (2-3). pp. 163-175.

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Abstract

Valinomycin is a highly flexible cyclic dodecadepsipeptide that transports ions across membranes. Such a flexibility in the conformation is required for its biological function since it has to encounter a variety of environments and liganding state. Exploration of conformational space of this molecule is therefore important and is one of the objectives of the present study that has been carried out by means of high temperature Molecular Dynamics. Further, the stability of the known bracelet-like structure of the uncomplexed valinomycin and the inherent flexibility around this structure has been investigated. The uncomplexed form of valinomycin has been simulated at 75–100 K for 1 ns in order to elucidate the average conformational properties. An alanine-analog of valinomycin has been simulated under identical conditions in order to evaluate the effect of sidechain on the conformational properties, The studies confirm the effect of sidechain on conformational equilibrium.

Item Type:	Journal Article
Publication:	Biophysical Chemistry
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	12 Jan 2010 05:07
Last Modified:	19 Sep 2010 05:53
URI:	http://eprints.iisc.ac.in/id/eprint/25213

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