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)
Full text not currently available from Enlighten.
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 |
University Staff: Request a correction | Enlighten Editors: Update this record