James H. Prestegard, Ph.D.
Complex Carbohydrate Research Center
|B.S. Chemistry||University of Minnesota||1966|
|Ph.D. Chemistry||California Institute of Technology||1971|
- Post-doctoral Experience
- Honors and Awards
- Georgia Research Alliance Eminent Scholar in NMR Spectroscopy
- Research Interests
- Research focuses on nuclear magnetic resonance (NMR) methods development and application of those methods to challenging problems involving soluble proteins, membrane proteins, cell-surface carbohydrates, and carbohydrate-protein interactions. Many of these systems are drug targets or involve interactions drugs might mimic.
An essential part of developing any new drug is to determine how that drug will bind to its target protein and to characterize the structures and conformations of the interacting molecules. Nuclear magnetic resonance (NMR) spectroscopy is rapidly becoming a major contributor of structural information on how natural ligands and derived drug candidates bind to protein targets. Both conventional NMR methodology (NOE based) and new methodology (RDC based) are used for retrieving this information.
- Representative Publications
- Seidel, R.D., Zhuang, T., and Prestegard, J.H. 2007. Bound-State Residual Dipolar Couplings for Rapidly Exchanging Ligands of His-Tagged Proteins. J. Am. Chem. Soc. 129: 4834-4839.
Wang, X., T. Weldeghorghis, G. Zhang, B. Imperiali, and J. H. Prestegard, 2008. Solution Structure of Alg13: The Sugar Donor Subunit of a Yeast N-Acetylglucosamine Transferase. Structure. 16: 965-975.
Zhuang, T., H-S Lee, B. Imperiali, and J. H. Prestegard. 2008. Structure determination of a Galectin-3-carbohydrate complex using paramagnetism-based NMR constraints. Protein Science. 17: 1220-1231.
Macnaughtan, M. A., Tian, F., Liu, S., Meng, L., Park, S., Azadi, P., Moremen, K. W. & Prestegard, J. H. 2008. C-13-sialic acid labeling of glycans on glycoproteins using ST6Gal-I. Journal of the American Chemical Society 130: 11864-11865.
Liu, Y., R.A. Kahn, and J.H. Prestegard. 2009. Structure and membrane interaction of myristoylated ARF1. Structure 17: 79-87.