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 BIOGRAPHY |
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Dr. Purich earned his Ph.D. in biochemistry at Iowa State University in 1972 for kinetically characterizing brain hexokinase. As a Staff Research Fellow at NIH, he investigated the control of the glutamine synthetase cascade. In 1973, Dr. Purich joined the Department of Chemistry, University of California Santa Barbara, where he rose to the rank of Professor and was awarded an Alfred P. Sloan Fellow in Chemistry, an NIH Research Career Development Award, and the Campus-wide Outstanding Teacher Award. In 1984, he became Chairman of our Department and resumed full-time activities as a Professor in 1996. Dr. Purich serves on the Journal of Biological Chemistry editorial board and as editor of Advances in Enzymology and a multi-volume treatise on enzyme kinetics and mechanism in Methods in Enzymology. He has also co-authored the 'Handbook of Biochemical Kinetics'. |
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RESEARCH DESCRIPTION |
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Our laboratory employs a battery of biochemical, biophysical and cellular methods to define the force-generating mechanisms responsible for actin-based motility during cell crawling and subcellular organelle
trafficking as well as microtubule-based motility during mitotic/meiotic chromosome disjunction and cilia/flagella biogenesis. We have discovered that these processes are actuated by novel cytoskeletal
end-tracking molecular motors that rely on actin monomer and tubulin heterodimer addition in the clamped-filament elongation of microfilaments and microtubules, respectively. In our actoclampin
model, "on-filament" ATP hydrolysis provides the free energy that drives clamp translocation in an affinity-modulated mecahnoenzyme (or energase)reaction. Among the techniques used are: video microscopy, FRET
microscopy, laser tweezers and particle-tracking microscopy, light scattering and fluorescence spectroscopy, enzyme kinetics, as well as
site-directed mutagenesis. This research, which is pursued collaboratively with Professor Richard Dickinson (Chemical Engineering), focuses on the motile properties of Listeria monocytogenes and other
biomimetic bead and vesicle systems to investigate actin-based motilitys well as the EB1-APC system to investigate tubulin-based motility.
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