Dr. Michael Silberstein

Dr. Michael Silberstein

My research is primarily focused on the identification and characterization of binding sites on proteins using the Computational Solvent Mapping methodology developed within the lab. This method utilizes multiple copies of various molecular fragments in order to locate favorable binding interactions that occur between these fragments and the protein. The locations where multiple fragment types overlap in contact with the protein are considered ‘consensus sites’, where it has been commonly shown that the most occupied consensus site generally correlates with the experimentally determined binding site. As a result, this methodology can be used to predict the location of binding sites, when such information has not yet been determined. Such an analytic tool will become increasingly more highly useful and informative as larger numbers of protein structures will be solved, as a result of various structural genomics initiatives, where the function and binding locations of specific protein targets may not be yet established.

My general research goals are to apply this unique methodology towards various protein targets of high interest to the biological community. I am currently working in collaboration with multiple experimental groups throughout the world so that this methodology can be used to address multiple hypotheses pertaining to the binding mechanisms involving various proteins with their specific ligands. Some examples of important systems that I have been currently working on using this method have included various protein Tyrosine Kinases (abl, src), Haloalkane Dehalogenases, Elastase, and Protein Tyrosine Phosphatase 1B, where general interest amongst the biological community regarding the protein’s specific biochemical interactions is high. I am also utilizing the mapping methodology towards additional biological binding mechanisms such as allostery and peptide binding interactions based on phage display in order to test the applicability of this method towards a wide range of biochemical processes.