Seminar on
Modern Optics and Spectroscopy


Christopher Cheatum, University of Iowa

Watching the protein mambo:
Fast enzyme dynamics

May 4, 2008

12:00 noon - 1:00 p.m. Grier Room 34-401


Abstract:

The structural dynamics of enzymes at the femtosecond to picosecond time scale have been invoked to explain the results of temperature-dependent kinetic-isotope-effect measurements for a number of enzymatic reactions.  We report studies of enzyme-ligand interaction dynamics at this time scale.  To identify the residues that control the dynamics, we have probed the fluctuations of isozymes and mutants of human carbonic anhydrase. We have also studied enzyme dynamics in a transition-state-analog complex for the enzyme formate dehydrogenase.  Our results support a potential role for fast dynamics near the transition state and reveal differences in the nature of enzyme-ligand interaction dynamics in the ground state and in vicinity of the transition state of a reaction.

TUESDAYS, 12:00-1:00, GRIER ROOM (34-401)
Refreshments served following the seminar

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Co-sponsored by the George R. Harrison Spectroscopy Laboratory,
the Department of Electrical Engineering and Computer Science and
the School of Science, Massachusetts Institute of Technology.