Quantitative measurement of protease ligand conformation

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

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)105-109
Number of pages5
JournalJournal of Computer-Aided Molecular Design
Volume22
Issue number2
DOIs
Publication statusPublished - 19 Jan 2008
Externally publishedYes

Keywords

  • Conformation
  • Inhibitor
  • Ligand
  • Measurement
  • Protease

ASJC Scopus subject areas

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

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