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Ph.D. 1964-University of Illinois
Biophysical and Biochemical characterization of proteins which recognize, interact with, and modulate other protein molecules is the focal point of the work done in our laboratory. Diverse biological phenomena-the regulation of enzymes by polypeptide activators and inhibitors, the intracellular partitioning of enzymes between soluble and particulate structures, and the reversible phosphorylation-dephosphorylation catalyzed by protein kinases and phosphoprotein phosphatases-entail specific protein-protein nteractions.
Specific areas of investigation include: (1) characterization of specific complexes formed by the Ca2+ binding protein calmodulin with biologically active peptides and enzyme-derived fragments; (2) investigation of the significance of the phosphorylation sites of muscle phosphofructokinase; and the role of Ca2+ binding proteins in the phosphorylation reaction; (3) characterization of oxidative modifications of calmodulin; (4) development and application of fluorometric assays for protein kinases and phosphoprotein phosphatases.