Chemistry Faculty:
James H. Prestegard,
Ph.D.
Professor
Phone: 706-542-6281
E-mail: jpresteg@ccrc.uga.edu
Biographical Information
B.S., University of Minnesota, 1966
Ph.D., Caltech, 1971
Yale University Faculty, 1970-1997
Research Interests
The advent of ultra high field magnets for NMR spectroscopy has opened important new avenues for understanding structure-function relationships in biological systems. Historically NMR has offered several advantages over other structural methods; it can be applied in a variety of environments, including aqueous solution and membrane phases; it can focus on particularly interesting features, such as the active site of a metalloprotein; and it can provide dynamic, as well as structural, information. Nevertheless, most structural applications have been limited by the dependence of NMR structural methods on data attainable only for smaller soluble biomolecules. Higher fields offer new sources of structural information that may change this situation. We are developing new NMR methodology and exploiting new, very high field, NMR facilities in order to explore this possibility.
Among the problems targeted for application of the new methods are ones related to how macromolecules function at the surfaces of biological membranes, how carbohydrates mediate cell-cell interactions, and how proteins interact with other proteins in the course of a biological process. At the heart of many current methods is the use of residual dipolar couplings. These novel observables return information on relative orientation of elements of interacting systems. They have also become the basis of a new structure determination protocol that is playing an important role in structural genomics efforts at the University of Georgia.
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Publications
- Adams, M. W. W., H. Dailey, L. J. DeLucas, M. Luo, J. H. Prestegard, J. P. Rose, and B. C. Wang. 2003. The Southeast Collaboratory for Structural Genomics: A high-throughput gene to structure factory. Acc. Chem. Res. 36: 191-198.
- Jain, N., S. Noble, and J. H. Prestegard. 2003. Structural characterization of a mannose binding protein-trimannoside complex using residual dipolar couplings. J. Mol. Biol. 328: 451-462.
- Glushka, J., M. Terrell, W. S. York, M. A. O’Neill, A. Gucwa, A. G. Darvill, P. Albersheim, and J. H. Prestegard. 2003. Primary structure of the 2-O-Me-_-L-fucose-containing side chain of the pectic polysaccharide rhamnogalacturonan II. Carbohydr. Res. 338: 341-352.
- Umemoto, K., H. Leffler, A. Venot, H. Valafar, and J.H. Prestegard. 2003. Conformational differences in liganded and unliganded states of Galectin-3. Biochemistry 42: 3688-3695.
- Bougault, C., M. K. Eidsness, and J. H. Prestegard. 2003. Hydrogen bonds in rubredoxins from mesophilic and hyperthermophilic organisms. Biochemistry 42: 4357-4372.
- Valafar, H., and J. H. Prestegard. 2003. Rapid classification to a protein fold family using a statistical analysis of dipolar couplings. Bioinformatics 19: 1-8.
- Kishore, A. I., and J. H. Prestegard. 2003. Molecular orientation and conformation of phosphatidylinositides in membrane mimetics using variable angle sample spinning (VASS) NMR. Biophys. J. 85: 4023-4040.
- Morris, L. C., H. Valafar, and J. H. Prestegard. 2004. Assignment of protein backbone resonances using connectivity, torsion angles and 13Ca chemical shifts. J. Biomol. NMR 29: 1-9
- Bougault, C., L. Feng, J. Glushka, E. Kupce, and J. H. Prestegard. 2004. Quantitation of rapid proton-deuteron amide exchange using Hadarmard spectroscopy. Biomol. NMR 28: 385-390.