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Prof. B.D. Nageswara Rao - General Colloquium
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October 10, 2002
Prof. B.D. Nageswara Rao, IUPUI
Exploring Enzyme Action Through Nuclear Magnetic Resonance
The molecular basis of enzyme action is one of the fundamental questions of biochemisty. A generally accepted paradigm of biomolecular science is that the answer to this question lies in the active-site structures of the enzymes i.e., the precise conformational arrangment of the enzyme-bound substrates and their amino-acid environment. For some time now, we have been involved in characterizing these structures for ATP-utilizing enzymes (ATP-adenosine triphosphate) by using solution-phase nuclear magnetic resonance(NMR) methods. These enzymes occur in a variety of critical cellular processes, and they usually require Mg(II) as an obligatory component, irrespective of which part of ATP is cleaved during catalysis. Free in solution, ATP is a floppy molecule with multiple mobilities, and when bound to one of these enzymes, assumes a conformation appropriate for the specific catalytic activity. We devised a strategy for comprehensive structural characterization of the enzyme-bound reaction complexes using NMR methods, and implemented it to obtain complete and reliable structures. We now reached a point where we can address somewhat incisive questions regarding the relationship of the structures to the function of the enzymes. A general description of this journey in reaching this point will be given, along with a brief discussion of the future prognosis.