| 19f NMR as a Probe of Protein Structure and Conformational Changes in Nitrogen Regulatory Protein C from Salmonella Typhimurium | ||
| Jared T. Hammill, Chemistry, Franklin and Marshall College, 2702 Sage Wood Dr, Newtown Square, PA 19073 and Dr Ryan Mehl, Chemistry, Franklin and Marshall College, PO Box 3003, Lancaster, PA 17604 Bacteria sense and respond to environmental stimuli using a two component regulatory system. These systems are comprised of a number of distinct elements, namely histidine kinases, response regulators and in the case of phosphorelays, histidine phosphotransfer proteins (HPts). The system that we are currently investigating is Nitrogen Regulatory Protein C (NtrC), a positively acting bacterial transcription factor, makes up one unit of a two component regulatory system. The second unit in the NtrC's two component regulatory system, a sensor histidine kinase phosphorylates the amino (N)-terminal domain of NtrC protein when changes in nitrogen concentration are detected. This study consisted of site-specifically altering NtrC's sequence by the incorporation of an unnatural fluorinated amino acid to be used as a probe to investigate the structural rearrangements resulting from phosphorylation with varying levels of nitrogen using 19F NMR. Extended Abstract Status: Not Uploaded | ||