Quantitative measurement of protease ligand conformation

Illingworth, C. J.R. , Parkes, K. E. B., Snell, C. R. and Reynolds, C. A. (2008) Quantitative measurement of protease ligand conformation. Journal of Computer-Aided Molecular Design, 22(2), pp. 105-109. (doi: 10.1007/s10822-008-9173-z) (PMID:18204905)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Illingworth, Dr Chris
Authors: Illingworth, C. J.R., Parkes, K. E. B., Snell, C. R., and Reynolds, C. A.
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity
College of Medical Veterinary and Life Sciences > School of Infection & Immunity > Centre for Virus Research
Journal Name:Journal of Computer-Aided Molecular Design
Publisher:Springer
ISSN:0920-654X
ISSN (Online):1573-4951

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