Professor and Eminent Scholar BS – Chemistry – University of Minnesota – 1966 PhD – Chemistry – Caltech -1971 Office: 1077 CCRC Contact Phone Number: 542-6281 Lab: 1075 CCRC, 1045 CCRC, A126 Life Sciences Lab Phone: 706-542-0257 CCRC, 706-583-8192 Life Sciences Fax Number: 542-4412 E-mail: jpresteg@ccrc.uga.edu Additional Information / Lab Page

Research Interests

Structural and Functional Characterization of Biomolecules by NMR

Research in the Prestegard laboratory 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 and understanding the structural and functional consequences of interactions that mimic drug-biomolecule interactions is a key part of drug design. 

Nuclear magnetic resonance (NMR) spectroscopy is rapidly becoming a major contributor of structural and dynamic information on biomolecular systems.  The Prestegard laboratory is a leader in both the development and application of new NMR methods.  Recent developments include the use of residual dipolar couplings (RDCs), a rich source of orientational information, and new NMR/MS strategies for resonance assignment in large glycosylated proteins.  The laboratory also hosts major NMR facilities (including a 900 MHz facility) that contribute to our ability to carry out research.

Selected Recent Publications

• Zhuang, T., H. Leffler, and J. H. Prestegard.  2006.  Enhancement of Bound-State Residual Dipolar Couplings: Conformational Analysis of Lactose Bound to Galectin-3. Protein Science. 15(7):  1780-1790.
  
  
• Yu, F. and J. H. Prestegard.  2006.  Structural Monitoring of Oligosaccharides through 13C Enrichment and NMR Observation of Acetyl Groups. Biophys. J.  91 (5):  1952-1959.
  
  
• Feng, L., R. Orlando, and J. H. Prestegard.  2006.  Amide proton back-exchange in deuterated peptides: Applications to MS and NMR analyses.  J Anal Chem. 78(19): 6685-6892.
  
  
• Wang, X., H-S Lee, F. E. Jenney, Jr., M. W. W. Adams, and James H. Prestegard.  2006. PF0610, a novel winged HTH variant possessing a rubredoxin-like Zn-ribbon motif from the hyperthermophilic archaeon, Pyrococcus furiousus.  Biochemistry 46: 752-761.
  
  
• Macnaughtan, M. A., M. Kamar, G. Alvarez-Manilla, A. Venot, Ph.D.; J. Glushka, J. M.  Pierce, and J. H. Prestegard.  2006. NMR Structural Characterization of Substrates Bound to N-Acetylglucosaminyltransferase V.  J.  Mol. Biol. 366(4): 1266-1281.
  
  
• Liu, S., Venot, A., Meng, L., Tian, F., Moremen, K.W., Boons, G-J and Prestegard, J.H. 2007. Spin-Labeled Analogs of CMP-NeuAc as NMR probes of the α-2,6-sialyltransferase ST6Gal Ι.  Chemistry & Biology 14: 409-418.
  
  
• 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.
  
  
• Feng, L., Lee, H-S., and Prestegard, J.H. 2007. NMR resonance assignments for sparsely 15N labeled proteins.  J. Biomol. NMR. 38:213-219.