Nuclear magnetic resonance (NMR) spin-relaxation studies enable us to explore enzyme function and protein dynamics:
1. What is the role of conformational exchange processes in enzyme function? 2. What are the contributions of dynamics to the energetics of ligand binding? 3. What is the pathway of propagation of ligand-induced dynamical changes?
Above mentioned questions are being investigated with a protein called VanX, one of the five proteins required for the vancomycin-resistant phenotype in clinically pathogenic gram-positive bacteria. Our investigation involves experiments utilizing not only solution NMR specroscopy, but also with a combination of chemical synthesis, computation, and directed biochemical studies to arrive at a self-consistent description of dynamics and function.
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