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<div><font face="Arial" color="#000000">Seminar on<br>
<b>Modern Optics and Spectroscopy<br>
<br>
<br>
Christopher Cheatum</b>,<br>
University of Iowa<br>
<br>
<i><b>Watching the protein mambo:<br>
Fast enzyme dynamics<br>
<br>
</b></i>March 4, 2008<br>
<br>
12:00 - 1:00 p.m.<br>
<br>
<br>
</font></div>
<div><font face="Lucida Grande" color="#000000">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.</font></div>
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