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Our primary focus is to understand the structure, function and dynamics of cAMP-dependent protein kinase (PKA) using biochemical, biophysical and recombinant approaches. The catalytic (C) subunit was the first protein kinase structure to be solved and continues to serve as a prototype for all protein kinases, now recognized as one of the largest gene superfamilies. In parallel with crystallography, kinetics, fluorescence, H/D exchange, and small angle Xray/neutron scattering are used to define conformational changes, ligand binding sites, and sites of protein:protein interaction.
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