Post-Doctoral CARB-NIST 2000; Post-Doctoral Hebrew University 1998; Ph.D. Maryland 1995
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The binding studies of a peptide mimic of the cytoplasmic tail of phospho-metarhodopsin II with rod arrestin (green). In blue we illustrate the calculated structure of the bound peptide and in red we illustrate the NMR structure of the bound peptide.
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The terahertz spectrum of bacteriorhodopsin, calculated from a harmonic normal mode analysis using CHARM22. A comparison with the experimental spectrum is illustrated in triangles and an example of the normal mode motion is illustrated for 30 cm-1
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The ability to predict key biological function, given the limited information currently available, requires a rather well developed understanding of biophysics. Developing methodologies that are predictive of such processes is the underlying theme of research in my group. We focus our work on three general areas of study; vibrational spectroscopy, small angle neutron scattering, and the visual process. While seemingly unrelated, all three areas cross-pollinate each other with ideas.
For example, we are developing a methodology to investigate the large scale anharmonic vibrational motion of proteins, specifically G-Protein Coupled Receptors (GPCRs). These proteins are involved in signal transduction pathways, such as the visual pathway. Therefore, developing a methodology that can elucidate vibrational dynamics, and hence large scale motion, will also aid in the study of the activation pathway in the visual process. Along the way, we are developing a method to treat vibrational motion in crystals, or other high symmetry materials. Why, because GPCRs are membrane proteins and someday, the membrane will have to be accounted for in our study of the visual process.Determining macromolecular structure, in solution, lies at the heart of (biological) small angle neutron scattering experiments (SANS). We are developing molecular coarse graining methods to interpret these scattering profiles. Our coarse graining methods are at a high enough resolution to capture the physical characteristics of the system, but yet reduced enough in dimensionality so as to be relevant for dynamics studies as well.
Finally, the study of the visual process is really a study of protein structure, dynamics and interactions. This study began with a peptide-protein Monte Carlo Simulated Annealing optimization algorithm and now encompasses a study of vibrational spectroscopy and in the future will apply the ideas of coarse graining in order to elucidate a rather complicated biological process.
