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Quantitative measurement of protease ligand conformation

Illingworth, Christopher JR and Parkes, Kevin EB and Snell, Christopher R and Reynolds, Christopher A (2008) 'Quantitative measurement of protease ligand conformation.' Journal of Computer-Aided Molecular Design, 22 (2). pp. 105-109. ISSN 0920-654X

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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
Uncontrolled Keywords: conformation; inhibitor; ligand; measurement; protease
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Science and Health
Faculty of Science and Health > Life Sciences, School of
SWORD Depositor: Elements
Depositing User: Elements
Date Deposited: 07 Oct 2011 14:36
Last Modified: 15 Jan 2022 00:31

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