Professor Robert T. Kennedy of the University of Michigan Ann Arbor is supported by the Analytical and Surface Chemistry Program in the Division of Chemistry to develop capillary electrophoresis methods to detect and quantify protein-protein interactions and to measure enzymatic activity. The model binding systems that will be investigated include G proteins, regulators of G protein signaling (RGS proteins), and SH2-domain proteins that bind phosphoproteins. The enzymatic systems include G-protein hydrolysis of GTP and adenylyl cylcase catalyzed formation of cyclic-AMP. Detection of the effects of receptor agonists and protein regulators of these reactions will be demonstrated. Life processes rely on affinity interactions between proteins to regulate when and where chemical reactions occur in cells. Advancements in understanding the chemistry of life rely on methods, such as those developed here, for quantifying affinity interactions. The methods will also be adapted to screening of natural product mixtures and libraries of pharmaceuticals for high-throughput discovery of drugs that alter these interactions. The work will involve high-level training of students with experience in both instrument development and biochemistry to support the scientific infrastructure.
