Research Description

Our research is focused on the development of multidimensional magic-angle spinning solid-state NMR techniques and their application to the analysis of molecular structure, conformational dynamics and intermolecular interactions of otherwise intractable biological macromolecules that are of fundamental importance to human health with the goal of understanding biological mechanism and function. We also employ solution-state NMR, cryo-electron microscopy and other complementary biophysical, computational, biochemical and molecular biology methods in support of our various research projects. Current research directions in the group include:

• Characterization of chromatin structure, dynamics and interactions with particular focus on the role of dynamic histone protein tail domains in mediating chromatin compaction and interactions with regulatory proteins
• Characterization of DNA base pairing in nucleosomes and other large protein-DNA complexes
• Elucidation of the structural basis of protein conformational inheritance in amyloid and prion diseases
• Development of conventional and dynamic nuclear polarization enhanced solid-state NMR methods for site-resolved measurement of structural and dynamic parameters in proteins with improved precision and accuracy
• Development of solid-state NMR methods for probing long range structure in biological macromolecules via incorporation of covalent paramagnetic tags 

Our work is currently funded by the National Science Foundation, the National Institutes of Health, Eli Lilly and the Evans Disease Endowment Fund at Ohio State.