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Knowledge of relevant structures has always been an essential component in our understanding of important biological processes, whether this knowledge relates to the anatomy of organisms, the ultrastructure of cells or precise details of molecular interactions.
Over the past 30 years, advances in X-ray crystallography and the development of high-field NMR spectroscopy have made it possible to observe atomic-level details of the structures of biologically important macromolecules, both in the crystal state and in solution. Such observations have, in turn, allowed the construction of sophisticated and experimentally testable models describing how these molecules function.
Examples of this abound: one outstanding example is the insight into genetics gained from the structure of the DNA double helix. In the Department of Molecular Genetics we have long recognized the necessity of high-resolution structural analysis for our understanding of virtually all cellular events.
The department has assembled an outstanding group of investigators having in common an interest in understanding the relationships among structure, dynamics and function in macromolecules.
We have world-class NMR and X-Ray facilities staffed by faculty with interests in signal transduction, protein folding, nucleic acid structure, protein dynamics, bacterial pathogenesis, and technique development. Our NMR facility houses five state-of-the-art spectrometers, with field strengths ranging from 400 to 800 MHz. Our X-ray facility houses a RigakuMSC MicroMax-007 microfocus X-ray generator with Osmic VariMax HR high-resolution optics, an R-axis-IV++ image plate detector, and an X-stream cryosystem. We also have state of the art crystallization robots for high-throughput screening to facilitate the growth of macromolecular crystals. Full computational support necessary to determine high resolution structures and molecular modeling is available.
The department also houses an array of instrumentation for biophysical analyses of macromolecules in solution. We have an analytical ultracentrifuge with absorbance and interference optics (one of only two in the state of Ohio), an isothermal titration calorimeter, circular dichroism/fluorescence and EPR spectrophotometers, and a dynamic light scattering instrument.
These biophysical approaches are complementary to structural techniques such as crystallography and NMR, and are used to characterize proteins in solution in preparation for structural analysis.
More information on faculty members with research interests in Structural Biology and Protein Structure/Function.
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