Associate Professor of Biochemistry & Molecular Biology
College of Medicine
Robert McKenna is convinced the only way to truly understand the physical interactions that govern “life” processes is to have a deep understanding of these interactions at the atomic level. This allows us to design new compounds with specific interactions with the disease target molecule, or rational drug design. McKenna has found that we still know very little “visually” on the structural role of solvent, hydrogen bonding, and protonation states of these macromolecular structures, as most of our understanding of these systems comes from molecular dynamic work.
McKenna’s studies use the most technologically advanced national and international X-ray synchrotron and neutron reaction and spallation sources, as these billion-dollar facilities are the only sources that allow us to visualize such interactions. McKenna has worked tirelessly to initially set up and then maintain the X-ray crystallography facility in the McKnight Brain Institute. Although this is a key resource for his research program, this facility is also used by many other investigators in the college and on the University of Florida campus.
McKenna’s lab has had the recent good fortune of obtaining crystals of the protein carbonic anhydrase, suitable for ultra-high X-ray and neutron diffracting studies. As a result, his lab has just joined a very elite group of structural studies that will permit the atomic mapping of most (if not all) hydrogen atoms of this protein. These detailed neutron structural studies will feed molecular dynamic studies to truly understand the thermal motions within the structure, the catalytic mechanism of the enzyme, the proton transfer event, and also provide a detailed mapping of the active site for in silico inhibitor design for the next generation of anti-cancer drugs.