Quantitative measurement of protease ligand conformation

Christopher J.R. Illingworth, Kevin E.B. Parkes, Christopher R. Snell, Christopher A. Reynolds

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)105-109
Number of pages5
JournalJournal of Computer-Aided Molecular Design
Issue number2
Publication statusPublished - 19 Jan 2008
Externally publishedYes


  • Conformation
  • Inhibitor
  • Ligand
  • Measurement
  • Protease

ASJC Scopus subject areas

  • Drug Discovery
  • Computer Science Applications
  • Physical and Theoretical Chemistry


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