Professor of Chemistry
University of Illinois, PhD
University of Pittsburgh, BSc
Our research is directed towards an understanding of non-covalent interactions in chemical and biochemical systems. We employ a variety of techniques in our work, but nuclear magnetic resonance is our most important tool. NMR can be used to obtain structures of complex macromolecules and is sensitive to molecular dynamics over a wide range of time scales. Equally important is the ability of NMR to provide information concerning intermolecular interactions via nuclear Overhauser effects. Combining NMR with other experimental and computational methods, we are actively investigating the following areas:
- Enzymes in the methionine salvage pathway: structure and function
- Monooxygenase enzyme systems: structure and dynamics
- Closed-shell ion pair structure and dynamics
- Amino acid interaction free energies for protein folding simulations: experimental and theoretical considerations
"Detection of substrate-dependent conformational changes in the P450 fold by nuclear magnetic resonance." Colthart AM, Tietz DR, Ni Y, Friedman JL, Dang M, Pochapsky TC. Sci Rep. 6:22035 (2016).
"Metal-Dependent Function of a Mammalian Acireductone Dioxygenase." Deshpande AR, Wagenpfeil K, Pochapsky TC, Petsko GA, Ringe D. Biochemistry. 55(9):1398-407 (2016).
"From intrinsically disordered protein to context-dependent folding: The α-synuclein tetramer is teased out of hiding." Pochapsky TC. Proc Natl Acad Sci U S A. 112(31):9502-3 (2015).
"Unfolding a molecular trefoil derived from a zwitterionic metallopeptide to form self-assembled nanostructures." Zhang Y, Zhou N, Shi J, Pochapsky SS, Pochapsky TC, Zhang B, Zhang X, Xu B. Nat Commun. 6:6165 (2015).