Are you interested in Disease? Development? Cell Signaling? Immunology? Drugs? Toxins? How cells interact with the environment or respond to stress? Then you have come to the right place. All of Life's processes begin and end at the molecular level and involve proteins. If you want to truly understand life, you need a solid foundation in the protein structure-function relationship. Proteins are remarkably diverse polymers that control all of life's essential processes. Because of the small size of proteins, understanding the chemistry of life is a challenging problem; the period at the end of this sentence could easily fit 1,000,000 average protein molecules placed end-to-end! My lab uses a combination of powerful techniques to discover how proteins work. X-ray crystallography allows us to examine the structure of proteins at atomic resolution, and with today's software and tools, even the undergraduates working in my lab routinely solve protein structures. Imagine having an interesting mutation in your favorite protein and having the ability to SEE what it did to the structure and function of the protein, and use that information to plan exciting experiments. The fastest turnaround we have had was protein to crystal to structure in less than 24 hours! We also use sedimentation velocity experiments to study the how the size and shape of the protein changes under specific conditions. This is the highest resolution technique for studying the oligomer structure of proteins, and it has turned into an amazing tool for studying one of our favorite allosteric proteins, UGDH. To see proteins in action, we use a variety of spectroscopic techniques. This includes steady state and transient state kinetics which allow us to observe proteins in action and learn about how they interact with a ligand or substrate, or study how allosteric regulation works, or even test a new mutation that you designed using the crystal structure of your favorite protein. The results of these and other experiments serve as puzzle pieces that we assemble into testable models that describe how proteins work. This is where the real fun begins! Because our projects are ripe with questions, and the proteins are amenable to so many techniques, it is trivial to generate and test new, interesting hypotheses and produce publishable results. In fact, my graduate students average about five years in the program and not a single one has defended their PhD with less than two first-author publications in press (and several co-authorships). In fact, I have had nine undergraduates listed on publications as either first- or co-author! Current projects in the lab include fundamental questions about protein mechanism and function, cancer metastasis, drug resistance and drug metabolism, and how complex glycans are assembled on proteins.
