Protein Electrostatics

We have developed the necessary SW to visualize the electrostatic fields that surround proteins as a function of e.g. pH or other parameters describing the protein environment. This allows us to investigate possible mechanisms that may explain pH dependent changes in enzymatic activity and recently we have been able to relate these calculations with protein stability as well. The method relies on the availability of a 3D structure of the protein in question. We have proposed novel mechanisms for product release in triglyceride lipases and esterases using this approach. The challenge ahead is to be able to make such calculations for proteins residing on an interface, thus mimicking e.g. a membrane protein. (Teresa Neves Petersen, Peter Fojan, Steffen B. Petersen)