Minority Research Planning Grant - Spectroscopic Studies of the Interaction of the c-Src SH3 Domain With Proline-Rich Peptides

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The goal of this project is to identify structural changes induced by the interaction between the SH3 domain of the c-Src protein and proline-rich peptides. To achieve these goals, flourescence resonance energy transfer (FRET) and fourier transformed infrared (FTIR) spectroscopies will be used. FRET experiments will provide information about distances involved in ligand binding to the SH3 domain hydrophobic groove. The SH3 domain-binding groove contains a conserved tryptophan residue, which will be the focus of the experiments proposed. FTIR experiments will allow us to study conformational changes in both the protein and the peptide upon complex formation. The combination of these studies will allow delineation of molecular interactions between SH3 domains and proline-rich peptides. Broader Impact: The proposed work is particularly well suited for the environment at the James Madison University. The P.I. has extensive experience working with proteins and protein characterization. The Chemistry Department has a number of undergraduate majors who are very interested in pursuing research during the academic year as well as the summer months. Moreover, the SH3 domain-containing proteins are suitable for use by undergraduate students. They are water-soluble proteins and their purification from the expression plasmids yield large amounts of protein. The undergraduate students will learn protein purification and protein engineering techniques. Additionally, students will gain experience in spectroscopic techniques, including fluorescence and FTIR. The exposure to different research techniques as well as training in logical problem solving will give students access to new science career paths. Additionally, some of the proposed experiments will form part of the schedule of activities for a general biochemistry laboratory course.