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.
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Illingworth, C.J.R., Parkes, K.E.B., Snell, C.R. et al. Quantitative measurement of protease ligand conformation. J Comput Aided Mol Des 22, 105–109 (2008). https://doi.org/10.1007/s10822-008-9173-z
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DOI: https://doi.org/10.1007/s10822-008-9173-z