The electrostatics of protein active sites can inform ligand design and SAR. However, no calculation of electrostatic potentials in the active site can be complete without also considering whether water molecules are tightly bound and contributing to the potentials and ligand binding. In this poster we will explore the effect of including water molecules shown to be energetically favorable on the electrostatic potential of individual proteins. We will present a new application to enable rapid and accurate calculation of water stability and protein interaction potentials. Combining these analyses with the popular Waterswap technique results in an in-depth knowledge of protein targets and ligand protein binding.

Putting electrostatics and water at the center of structure-based drug design

253rd National Meeting (2017)

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