Jeff Peng, University of Notre Dame
Proteins often bind small molecules modulators or substrates with dynamic substructures. Knowing how the internal motions of these substructures change upon substrate binding can help guide inhibitor design. NMR spectroscopy is an attractive means for identifying these changes, as it can profile sequence-specific changes over a broad time scale. Accordingly, this presentation will discuss our NMR studies of bacterial proteins supporting resistance to beta-lactam antibiotics. While our findings are still restricted mainly to the protein backbone, they suggest enhanced protein flexibility can amplify antibiotic resistance.