Ph.D., Syracuse University, 1986
Phone: 718-951-5000 x2847
Grant Support: NIH: $953,847; subcontract: $191,634
Nature of Research
My research involves structural and functional studies of the bone protein osteocalcin complexed to Ca2+, Pb2+ and Mg2+. Osteocalcin is involved in bone remodeling and crystal size. We are investigating the function of osteocalcin by observing mineral binding properties in the presence of different metal ions. Alterations in detailed bone mineral properties and bone strength as a consequence of protein mineral binding are determined by Fourier Transform IR Microscopy and biomechanical measurements. Cortical and trabecular bone density are determined by microCT. Results are relevant to the molecular mechanism of Pb2+ toxicity, diabetes and bone biology.
A second project involves the structural and functional studies of the gap junction protein Connexin. Gap junctions between cells are composed of 6 Connexin molecules. We are interested in the molecular mechanism of voltage gating in gap junctions. Electrophysiological techniques are used to assess the voltage gating of the channels. We use 2D NMR techniques to determine the structure of N-terminal peptides of wildtype and mutant Connexins which form functional or nonfunctional channels. By comparing these structures a molecular mechanism of voltage gating is developed.
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