Research Interests

I am a protein chemist and structural biologist who studies protein phosphorylation. Specifically, I have characterized the structure and function of cAMP-dependent protein kinase, one of the simplest members of a large family of enzymes that are critical on/off switches for most signal transduction pathways. A multidisciplinary strategy was demanded. Solving the first protein kinase crystal structure was a milestone that provided a template for the entire family of several thousand enzymes. By combining crystallography and fluorescence, we are now defining the molecular motions of this enzyme. The structure of the regulatory cAMP receptor protein was also solved. Both subunits are targets for drug design. In parallel with structure analysis, fluorescence strategies were developed to follow the trafficking of these proteins in living cells. This led to the discovery of novel nuclear export signals that actively export proteins from the nucleus. The recent discovery of novel proteins that anchor the kinase to mitochondria and other organelles adds a further dimension to the assembly of this signaling pathway. Using PKA to model other kinases, to define docking motifs, and as a template for drug design, is also allowing us to couple technological advances in computation with important biological questions.

Membership Type


Election Year


Primary Section

Section 21: Biochemistry

Secondary Section

Section 29: Biophysics and Computational Biology