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Quantitative measurement of protease ligand conformation

Illingworth, CJR and Parkes, KEB and Snell, CR and Reynolds, CA (2008) 'Quantitative measurement of protease ligand conformation.' Journal of Computer-Aided Molecular Design, 22 (2). 105 - 109. ISSN 0920-654X

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Abstract

The tendency for protease ligands to bind in an extended conformation has been suggested as an important factor for the identification of compounds of medicinal importance. Here we present a novel graph-theoretical method giving a quantitative measure of ligand conformation, and through application of this method to a representative set of protease ligands in bound and unbound conformations, derive the result that protease ligands are more extended in conformation when in their bound state. © Springer Science+Business Media B.V. 2008.

Item Type: Article
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Science and Health > Biological Sciences, School of
Depositing User: Jim Jamieson
Date Deposited: 07 Oct 2011 14:36
Last Modified: 17 Aug 2017 18:17
URI: http://repository.essex.ac.uk/id/eprint/940

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