Dr. Jeremy Smith is the first Governor's Chair at the University of Tennessee and the Director of UT/ORNL Center for Molecular Biophysics (CMB) at Oak Ridge National Laboratory. Dr. Smith applies computer simulations to important physical, chemical and biological questions. He has published over 200 peer-reviewed scientific articles on different topics, and specializes in enzyme catalysis and bioenergetics. CMB, directed by Dr. Smith, sits at the interface between the Biological and Environmental, Physical, Computational and Neutron Scattering Directorates at ORNL. One of the main goals of CMB is to apply high-performance computational simulations and neutron science to determine catalytic processes involving enzymes and synthetic models/complexes and to understand reaction mechanisms and origin of catalytic effects. CMB has a keen interest in collaborating with experimental labs to help to improve efficiencies of existing catalysts or design new ones (e.g., enzyme mimics). CMB consists of several UTK faculty members and ORNL staff scientists, postdoctoral associates, as well as graduate and undergraduate students.
Selected current research themes include:
Environmental remediation: Understanding catalytic mechanisms and actions of key bacterial enzymes (proteins) and synthetic models for the purpose of restoring mercury contaminated environments.
- Bioenergy: Studying synergistic actions of enzyme complexes on cellulose and understanding recalcitrance of cellulose to hydrolysis for developing cost effective strategies of deconstructing cellulosic biomass.
- Catalytic mechanisms of enzymes: A number of enzymes that catalyze biologically important reactions are currently under investigations by the members of CMB. The enzymes and processes studied include (but not limited to) (1) The molecular motor myosin and the mechanism of myosin ATP hydrolysis; (2) Specificities and mechanisms of histone-modifying enzymes in their writing of epigenetic marks; (3) Acid proteases: mechanisms, specificities and activations; (4) Enzymatic deamination of cytidine (cytosine) and adenosine; (5) Restriction enzymes.