Almost all biochemical reactions take place in aqueous solution. In order to understand properties such as stability and interactions in the binding pocket of a protein, it is essential to find an accurate description of the thermodynamics of the solvation process. This knowledge enables the identification of binding sites and the prediction of binding affinities of a protein and can drastically accelerate the first steps in drug development Therefore, part of our research focusses on the active development of Grid Inhomogenous Solvation Theory (GIST), a computational method that calculates the statistical solvent properties of grid points of a grid stretched around the molecule of interest.
