The binding of small molecules to proteins is accompanied by displacement of water molecules from protein hydration sites. The thermodynamic properties of these hydration sites can be predicted using the statistical mechanical method of inhomogeneous fluid solvation theory (IFST). We have analysed the predictions of IFST based on molecular dynamics simulations and compared them with the binding modes of small molecules for a number of test cases. This has allowed us to assess druggability and rationalise the observed binding modes. Particular emphasis has been placed on the analysis of small molecule binding to surfaces involved in protein-protein interactions.

Predicting the displacement of water molecules from protein hydration sites due to small molecule binding

245th National Meeting (2013)

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