title: Quantitative measurement of protease ligand conformation.
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.
authors.affiliation: Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK.
authors.forename: Christopher J R
authors.initials: CJ
authors.lastname: Illingworth
authors.forename: Kevin E B
authors.initials: KE
authors.lastname: Parkes
authors.forename: Christopher R
authors.initials: CR
authors.lastname: Snell
authors.forename: Christopher A
authors.initials: CA
authors.lastname: Reynolds
mesh_terms: D008024:Ligands; D008958:Models, Molecular; D008968:Molecular Conformation; D010447:Peptide Hydrolases / Q000378:metabolism*
chemical_list: D008024:Ligands; D010447:Peptide Hydrolases