Emeritus Professor

Contact Info

Office:
1077ccrc
Phone Number:
Lab Office:
706-542-0257
Education:
  • B.S., University of Minnesota, 1966
  • Ph.D., Caltech, 1971
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 an enzyme; 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. We are also exploring the use of new hyperpolarization devices to improve NMR sensitivity, particularly for monitoring the metabolic products of enzymatic reations.  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, how proteins interact with other proteins in the course of a biological process, and how metabolic profiles can report on disease. See our group website for recent examples of research projects.

Selected Publications:

 

Moure, M. J., Zhuo, Y., Boons, G. J., & Prestegard, J. H. (2017). Perdeuterated and  13 C-enriched myo-inositol for DNP assisted monitoring of enzymatic phosphorylation by inositol-3-kinase. Chem. Commun.. doi:10.1039/C7CC07023C

Sheikh, M. O., Thieker, D., Chalmers, G., Schafer, C. M., Ishihara, M., Azadi, P., . . . West, C. M. (n.d.). O2 sensing associated glycosylation exposes the F-box combining site of the Dictyostelium Skp1 subunit in E3 ubiquitin ligases. Journal of Biological Chemistry, jbc.M117.809160. doi:10.1074/jbc.M117.809160

Zhuo, Y., Cordeiro, C. D., Hekmatyar, S. K., Docampo, R., & Prestegard, J. H. (2017). Dynamic nuclear polarization facilitates monitoring of pyruvate metabolism in Trypanosoma brucei. Journal of Biological Chemistry, 292(44), 18161-18168. doi:10.1074/jbc.M117.807495

Pederson, K., Chalmers, G. R., Gao, Q., Elnatan, D., Ramelot, T. A., Ma, L. -C., . . . Prestegard, J. H. (2017). NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with 13C-methyl alanine. Journal of Biomolecular NMR, 68(3), 225-236. doi:10.1007/s10858-017-0123-8

Thieker, D. F., Chalmers, G., Xu, X., Sheikh, M. O., Glushka, J. N., Prestegard, J. H., . . . West, C. M. (2017). Structural Effects of Skp1 Glycosylation. In FASEB JOURNAL Vol. 31 (pp. 2 pages). Chicago, IL: FEDERATION AMER SOC EXP BIOL. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000405461403324&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Gao, Q., Chalmers, G. R., Moremen, K. W., & Prestegard, J. H. (2017). NMR assignments of sparsely labeled proteins using a genetic algorithm. JOURNAL OF BIOMOLECULAR NMR, 67(4), 283-294. doi:10.1007/s10858-017-0101-1

Liu, Y., Sharp, J. S., Do, D. H. -T., Kahn, R. A., Schwalbe, H., Buhr, F., & Prestegard, J. H. (2017). Mistakes in translation: Reflections on mechanism. PLOS ONE, 12(6). doi:10.1371/journal.pone.0180566

Xu, X., Sheikh, M. O., Thieker, D., Schafer, C. M., Chalmers, G., Eletsky, A., . . . West, C. M. (2016). Role of the oxygen-dependent Skp1 glycan in Skp1 organization in Dictyostelium. In GLYCOBIOLOGY Vol. 26 (pp. 1417-1418). Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000392935600111&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Eletsky, A., Chen, C. -Y., Fong, J. J., Nizet, V., Varki, A., & Prestegard, J. H. (2016). NMR Structure of Streptococcal IgA-Fc Receptor Siglec-5 Binding Domain. In GLYCOBIOLOGY Vol. 26 (pp. 1410-1411). Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000392935600095&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Prestegard, J. H., Moremen, K. W., Gao, Q., & Chalmers, G. R. (2016). Characterizing Glycosylated Proteins and Their Interactions Using Sparse-Labeling NMR. In GLYCOBIOLOGY Vol. 26 (pp. 1461). Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000392935600214&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Prestegard, J., Moremen, K. W., Gao, Q., & Chalmers, G. (2016). Characterizing Glycosylated Proteins and Their Interactions Using Sparse-Labeling NMR. Poster session presented at the meeting of  Annual Meeting of the Society for Glycobiology.

Singh, A., Tessier, M. B., Pederson, K., Wang, X., Venot, A. P., Boons, G. -J., . . . Woods, R. J. (2016). Extension and validation of the GLYCAM force field parameters for modeling glycosaminoglycans. CANADIAN JOURNAL OF CHEMISTRY, 94(11), 927-935. doi:10.1139/cjc-2015-0606

Gao, Q., Chen, C. -Y., Zong, C., Wang, S., Ramiah, A., Prabhakar, P., . . . Prestegard, J. H. (2016). Structural Aspects of Heparan Sulfate Binding to Robo1-Ig1-2. ACS CHEMICAL BIOLOGY, 11(11), 3106-3113. doi:10.1021/acschembio.6b00692

Zhuo, Y., Yang, J. -Y., Moremen, K. W., & Prestegard, J. H. (2016). Glycosylation Alters Dimerization Properties of a Cell-surface Signaling Protein, Carcinoembryonic Antigen-related Cell Adhesion Molecule 1 (CEACAM1). JOURNAL OF BIOLOGICAL CHEMISTRY, 291(38), 20085-20095. doi:10.1074/jbc.M116.740050

Prestegard, J. H., Moremen, K., Zhuo, Y., & Yang, J. -Y. (2016). Glycosylation Alters Oligomerization Status of the Human CEACAM1-IgV Domain. In FASEB JOURNAL Vol. 30 (pp. 1 page). San Diego, CA: FEDERATION AMER SOC EXP BIOL. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000406444007296&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Prestegard, J. H., Moremen, K., Zhuo, Y., & Yang, J. -Y. (2016). Glycosylation Alters Oligomerization Status of the Human CEACAM1-IgV Domain. In FASEB JOURNAL Vol. 30 (pp. 1 page). San Diego, CA: FEDERATION AMER SOC EXP BIOL. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000406444003370&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Chalmers, G., Glushka, J. N., Foley, B. L., Woods, R. J., & Prestegard, J. H. (2016). Direct NOE simulation from long MD trajectories. JOURNAL OF MAGNETIC RESONANCE, 265, 1-9. doi:10.1016/j.jmr.2016.01.006

Franks, J., Glushka, J. N., Jones, M. T., Live, D. H., Zou, Q., & Prestegard, J. H. (2016). Spin Diffusion Editing for Structural Fingerprints of Therapeutic Antibodies. ANALYTICAL CHEMISTRY, 88(2), 1320-1327. doi:10.1021/acs.analchem.5b03777

Park, Y., Jowitt, T. A., Day, A. J., & Prestegard, J. H. (2016). Nuclear Magnetic Resonance Insight into the Multiple Glycosaminoglycan Binding Modes of the Link Module from Human TSG-6. BIOCHEMISTRY, 55(2), 262-276. doi:10.1021/acs.biochem.5b01148

Everett, J. K., Tejero, R., Murthy, S. B. K., Acton, T. B., Aramini, J. M., Baran, M. C., . . . Montelione, G. T. (2016). A community resource of experimental data for NMR/X-ray crystal structure pairs. PROTEIN SCIENCE, 25(1), 30-45. doi:10.1002/pro.2774

Rosato, A., Vranken, W., Fogh, R. H., Ragan, T. J., Tejero, R., Pederson, K., . . . Vuister, G. W. (2015). The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013. JOURNAL OF BIOMOLECULAR NMR, 62(4), 413-424. doi:10.1007/s10858-015-9953-4

Deshauer, C., Morgan, A. M., Ryan, E. O., Handel, T. M., Prestegard, J. H., & Wang, X. (2015). Interactions of the Chemokine CCL5/RANTES with Medium-Sized Chondroitin Sulfate Ligands. STRUCTURE, 23(6), 1066-1077. doi:10.1016/j.str.2015.03.024

Queiroz, I. N. L., Wang, X., Glushka, J. N., Santos, G. R. C., Valente, A. P., Prestegard, J. H., . . . Pomin, V. H. (2015). Impact of sulfation pattern on the conformation and dynamics of sulfated fucan oligosaccharides as revealed by NMR and MD. GLYCOBIOLOGY, 25(5), 535-547. doi:10.1093/glycob/cwu184

Prestegard, J. (2015). Glycans on Glycoproteins: Insight into Function from NMR and MD. In Chemistry Department Seminar. Clemson, SC: Clemson University.

Prestegard, J. (2014). Glycans on Glycoproteins: Insight into Function from NMR and MD. In Departmental seminar. Boulder, CO: University of  Colorado.

Lemak, A., Wu, B., Yee, A., Houliston, S., Lee, H. -W., Gutmanas, A., . . . Arrowsmith, C. H. (2014). Structural Characterization of a Flexible Two-Domain Protein in Solution Using Small Angle X-Ray Scattering and NMR Data. STRUCTURE, 22(12), 1862-1874. doi:10.1016/j.str.2014.09.013

Pulavarti, S. V. S. R. K., Huang, Y. J., Pederson, K., Acton, T. B., Xiao, R., Everett, J. K., . . . Szyperski, T. (2014). Solution NMR structures of immunoglobulin-like domains 7 and 12 from obscurin-like protein 1 contribute to the structural coverage of the human cancer protein interaction network. Journal of Structural and Functional Genomics, 15(4), 209-214. doi:10.1007/s10969-014-9185-y

Prestegard, J. (2014). Conquering NMR Sensitivity Limitations: DNP-enhanced Studies of Cellular Metabolism. In UGA Department of Physics and Astronomy Colloquium. Athens, GA: University of Georgia.

Yang, Y., Ramelot, T. A., Lee, H. -W., Xiao, R., Everett, J. K., Montelione, G. T., . . . Kennedy, M. A. (2014). Solution structure of the free Z alpha domain of human DLM-1 (ZBP1/DAI), a Z-DNA binding domain. JOURNAL OF BIOMOLECULAR NMR, 60(2-3), 189-195. doi:10.1007/s10858-014-9858-7

Yang, Y., Ramelot, T. A., Lee, H. -W., Xiao, R., Everett, J. K., Montelione, G. T., . . . Kennedy, M. A. (2014). Solution structure of a C-terminal fragment (175-257) of CV_0373 protein from Chromobacterium violaceum adopts a winged helix-turn-helix (wHTH) fold. JOURNAL OF BIOMOLECULAR NMR, 60(2-3), 197-202. doi:10.1007/s10858-014-9860-0

Zhang, C., Zhuo, Y., Moniz, H. A., Wang, S., Moremen, K. W., Prestegard, J. H., . . . Yang, J. J. (2014). Direct Determination of Multiple Ligand Interactions with the Extracellular Domain of the Calcium-sensing Receptor. JOURNAL OF BIOLOGICAL CHEMISTRY, 289(48), 33529-33542. doi:10.1074/jbc.M114.604652

Pederson, K., Mitchell, D. A., & Prestegard, J. H. (2014). Structural Characterization of the DC-SIGN-Lewis(X) Complex. BIOCHEMISTRY, 53(35), 5700-5709. doi:10.1021/bi5005014

Prestegard, J. (2014). Glycans on Glycoproteins: Insight into Function from NMR and MD. In NMR Symposium. Thousand Oaks, CA: Amgen, Inc.

Prestegard, J. (2014). Following Metabolic Pathways with H-D Exchange and DNP NMR. In SECIM Metabolomics Workshop and Symposium. Gainesville, FL: University of  Florida.

Prestegard, J. (2014). Introduction to DNP. In SECIM Metabolomics Workshop and Symposium. Gainesville, FL: University of  Florida.

Prestegard, J. (2014). Protein-Protein Interactions at a Membrane Surface - NMR of the ARF1-FAPP1 System. In Biomolecular Structure, Dynamics, and Function: Membrane Proteins. Nashville, TN: Vanderbilt University.

Frank, M., Walker, R. C., Lanzilotta, W. N., Prestegard, J. H., & Barb, A. W. (2014). Immunoglobulin G1 Fc Domain Motions: Implications for Fc Engineering. JOURNAL OF MOLECULAR BIOLOGY, 426(8), 1799-1811. doi:10.1016/j.jmb.2014.01.011

Prestegard, J. H., Agard, D. A., Moremen, K. W., Lavery, L. A., Morris, L. C., & Pederson, K. (2014). Sparse labeling of proteins: Structural characterization from long range constraints. JOURNAL OF MAGNETIC RESONANCE, 241, 32-40. doi:10.1016/j.jmr.2013.12.012

Prestegard, J. (2014). Sparse-Labeling and Long-Range Constraints: Structure and Function of Glycoproteins. In 55th Annual Experimental NMR Conference. Boston, MA.

Liu, Y., Kahn, R. A., & Prestegard, J. H. (2014). Interaction of Fapp1 with Arf1 and PI4P at a Membrane Surface: An Example of Coincidence Detection. STRUCTURE, 22(3), 421-430. doi:10.1016/j.str.2013.12.011

Queiroz, I. N. L., Wang, X., Glushka, J. N., Santos, G. R. C., Valente, A. P., Prestegard, J., . . . Pomin, V. H. (2014). Impact of sulfation pattern on the conformation and dynamics of sulfated fucan oligosaccharides as revealed by NMR and MD. Glycobiology, cwu184.

Prestegard, J. (2013). Characterizing Glycoproteins and Protein-Glycan Complexes Using NMR. St. Louis, MO: Pfizer.

Pulavarti, S. V. S. R. K., Eletsky, A., Lee, H. -W., Acton, T. B., Xiao, R., Everett, J. K., . . . Szyperski, T. (2013). Solution NMR structure of CD1104B from pathogenic Clostridium difficile reveals a distinct α-helical architecture and provides first structural representative of protein domain family PF14203. Journal of Structural and Functional Genomics, 14(4), 155-160. doi:10.1007/s10969-013-9164-8

Prestegard, J. (2013). Investigating Glycosaminoglycan-Protein Interactions and how they Modulate Cellular Function. Augusta, Georgia: Medical College of Georgia.

Prestegard, J. (2013). Glycans on Glycoproteins - Insight into Function from NMR. Princeton, NJ: Princeton.

Prestegard, J. (2013). Structure and Dynamics of Large and Glycosylated Proteins Using Paramagnetic Tags. Chamonix, France.

Prestegard, J. (2013). Monitoring Enzymatic Conversion of DNP-Enhanced Substrates by Indirect Detection. In EUROMAR. Crete, Greece.

Prestegard, J. (2013). Glycoprotein Structure and Function from Sparse Labels and Paramagnetic Tags. University of Maryland, Rockville, MD.

Prestegard, J. (2013). Glycans in Immunoglobulin G: Structure and Dynamics from NMR. In 2013 Allinger Lecture. Athens, Georgia.

Barb, A. W., Hekmatyar, S. K., Glushka, J. N., & Prestegard, J. H. (2013). Probing alanine transaminase catalysis with hyperpolarized (CD3)-C-13-pyruvate. JOURNAL OF MAGNETIC RESONANCE, 228, 59-65. doi:10.1016/j.jmr.2012.12.013

Prestegard, J. (2013). An NMR View of Glycoprotein Glycan Structure and Function. In Biochemistry Department. New York, NY.

Prestegard, J. (2013). An NMR View of Glycoprotein Glycan Structure and Function. In Biochemistry  Seminar. New York, NY: City College of New York.

Pulavarti, S. V., Eletsky, A., Lee, H. W., Acton, T. B., Xiao, R., Everett, J. K., . . . Szyperski, T. (2013). Solution NMR structure of CD1104B from pathogenic Clostridium difficile reveals a distinct alpha helical architecture. J Struct Funct Genomics, 14, 155-160.

Barb, A. W., Wang, X., & Prestegard, J. H. (2013). Refolded recombinant Siglec5 for NMR investigation of complex carbohydrate binding. PROTEIN EXPRESSION AND PURIFICATION, 88(2), 183-189. doi:10.1016/j.pep.2013.01.005

Fahim, A., Mukhopadhyay, R., Yandle, R., Prestegard, J. H., & Valafar, H. (2013). Protein Structure Validation and Identification from Unassigned Residual Dipolar Coupling Data Using 2D-PDPA. MOLECULES, 18(9), 10162-10188. doi:10.3390/molecules180910162

Wang, X., Sharp, J. S., Handel, T. M., & Prestegard, J. H. (2013). Chemokine Oligomerization in Cell Signaling and Migration. In Unknown Book (Vol. 117, pp. 531-578). doi:10.1016/B978-0-12-386931-9.00020-9

Prestegard, J. H., Sahu, S. C., Nkari, W. K., Morris, L. C., Live, D., & Gruta, C. (2013). Chemical shift prediction for denatured proteins. JOURNAL OF BIOMOLECULAR NMR, 55(2), 201-209. doi:10.1007/s10858-012-9702-x

Prestegard, J. (2012). NMR in the Pursuit of Glycoprotein and Glycoprotein Glycan Structure. In Biochemsitry Department Seminar. Durham, NC: Duke University.

Prestegard, J. (2012). NMR in the Pursuit of Glycoprotein and Glycoprotein Glycan Structure. In Chemistry Department Colloquium. University Park, PA: Penn State University.

Prestegard, J. (2012). Long Range NMR Constraints in the Assembly of Protein-Carbohydrate Complexes. In Joint 41st SEMRC/SERMACS Symposium. Raleigh, NC: SEMRC/SERMACS.

Eletsky, A., Jeong, M. -Y., Kim, H., Lee, H. -W., Xiao, R., Pagliarini, D. J., . . . Szyperski, T. (2012). Solution NMR Structure of Yeast Succinate Dehydrogenase Flavinylation Factor Sdh5 Reveals a Putative Sdh1 Binding Site. BIOCHEMISTRY, 51(43), 8475-8477. doi:10.1021/bi301171u

Prestegard, J. (2012). NMR Approaches to the  Structure and Dynamics of Glycoproteins. In North Jersey American Chemical Society NMR Symposium. Piscataway, NJ: Rutgers University.

Barb, A. W., Ho, T. G., Flanagan-Steet, H., & Prestegard, J. H. (2012). Lanthanide binding and IgG affinity construct: Potential applications in solution NMR, MRI, and luminescence microscopy. PROTEIN SCIENCE, 21(10), 1456-1466. doi:10.1002/pro.2133

Ramelot, T. A., Rossi, P., Forouhar, F., Lee, H. -W., Yang, Y., Ni, S., . . . Kennedy, M. A. (2012). Structure of a Specialized Acyl Carrier Protein Essential for Lipid A Biosynthesis with Very Long-Chain Fatty Acids in Open and Closed Conformations. BIOCHEMISTRY, 51(37), 7239-7249. doi:10.1021/bi300546b

Prestegard, J. (2012). Glycan Remodeling on Glycoproteins: NMR Investigations of Structure and Dynamics. In 26th International Carbohydrate Symposium. Madrid, Spain: International Carbohydrate Organization.

Prestegard, J. (2012). Isotope Labeling in Mammalian HEK293 Expression Systems. In Northeast Structural Genomics Consortium Annual Meeting. New Brunswick, NJ: Rutgers University.

Prestegard, J. (2012). Introduction to DNP and DNP in Cells. In University of  Florida Metabolomics Workshop. Gainesville, FL: National High Magnetic Field Laboratory.

Barb, A. W., Meng, L., Gao, Z., Johnson, R. W., Moremen, K. W., & Prestegard, J. H. (2012). NMR Characterization of Immunoglobulin G Fc Glycan Motion on Enzymatic Sialylation. BIOCHEMISTRY, 51(22), 4618-4626. doi:10.1021/bi300319q

Prestegard, J. (2012). NMR Analysis Demonstrates that Immunoglobulin G N-Glycans are Accessible and Dynamic. In 41st Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology. Iguassu Falls, Parana, Brazil: SBBq.

Prestegard, J. (2012). NMR in the Structure and Function of Glycans, Glycan Binding Proteins and Glycoproteins. In Interdepartmental Seminar, Department of Organic Chemistry. Stockholm, Sweden: University of Stockholm.

Ertekin, A., Aramini, J. M., Rossi, P., Leonard, P. G., Janjua, H., Xiao, R., . . . Montelione, G. T. (2012). Human Cyclin-dependent Kinase 2-associated Protein 1 (CDK2AP1) Is Dimeric in Its Disulfide-reduced State, with Natively Disordered N-terminal Region. JOURNAL OF BIOLOGICAL CHEMISTRY, 287(20), 16541-16549. doi:10.1074/jbc.M112.343863

Prestegard, J. (2012). Structure Dynamics of Glycoproteins and Their Glycans by NMR. In Symposium on Recent Advances in Biomedical Sciences. Taipei, Taiwan: Academia Sinica.

Pomin, V. H., Park, Y., Huang, R., Heiss, C., Sharp, J. S., Azadi, P., & Prestegard, J. H. (2012). Exploiting enzyme specificities in digestions of chondroitin sulfates A and C: Production of well-defined hexasaccharides. GLYCOBIOLOGY, 22(6), 826-838. doi:10.1093/glycob/cws055

Eletsky, A., Petrey, D., Zhang, Q. C., Lee, H. -W., Acton, T. B., Xiao, R., . . . Szyperski, T. (2012). Solution NMR structures reveal unique homodimer formation by a winged helix-turn-helix motif and provide first structures for protein domain family PF10771. Journal of Structural and Functional Genomics, 13(1), 1-7. doi:10.1007/s10969-011-9121-3

Barb, A., Ho, T., & Prestegard, J. (2011). Assessing the conformational distribution and exposure of immunoglobulin G N-glycans using paramagnetic tags and NMR. In Annual Conference of the Society for Glycobiology. Seattle, WA: Society for Glycobiology.

Barb, A. W., Freedberg, D. I., Battistel, M. D., & Prestegard, J. H. (2011). NMR detection and characterization of sialylated glycoproteins and cell surface polysaccharides. JOURNAL OF BIOMOLECULAR NMR, 51(1-2), 163-171. doi:10.1007/s10858-011-9550-0

Prestegard, J. (2011). A dynamical view of IgG glycans using isotope labeling and NMR. In Frontiers in glycostructure and membrane biology. Borstel, Germany: Borstel Research Center.

Wang, X., Watson, C., Sharp, J. S., Handel, T. M., & Prestegard, J. H. (2011). Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data. STRUCTURE, 19(8), 1138-1148. doi:10.1016/j.str.2011.06.001

Liu, Y., & Prestegard, J. H. (2011). Multi-dimensional NMR without coherence transfer: Minimizing losses in large systems. JOURNAL OF MAGNETIC RESONANCE, 212(2), 289-298. doi:10.1016/j.jmr.2011.07.007

Barb, A., Ho, T., Prestegard, J., & Moremen, K. (2011). NMR analysis demonstrates the immunoglobulin G N-glycans are accessible and dynamic. In Consortium for Functional Glycomics Principal Investigators meeting. Bethesda, MD: National Institutes of Health.

Prestegard, J. (2011). Combining NMR with other technologies: chemokine aggregation and GAG interactions. In 35 Annual Steenbock Symposium. Madison, WI: University of Wisconsin.

Barb, A. W., Hekmatyar, S. K., Glushka, J. N., & Prestegard, J. H. (2011). Exchange facilitated indirect detection of hyperpolarized (ND2)-N-15-amido-glutamine. JOURNAL OF MAGNETIC RESONANCE, 212(2), 304-310. doi:10.1016/j.jmr.2011.07.008

Barb, A., & Prestegard, J. (2011). NMR analysis demonstrates the immunoglobulin g N-glycans are accessible and dynamic. In Gordon Carbohydrates Research Conference. Waterville, ME: Gordon Conferences.

Prestegard, J. (2011). Analysis of glycan structure and biosynthesis by NMR. In Alliance of Glycobiologists for Detection of Cancer and Cancer Risk. online seminar: National Cancer Institute.

Prestegard, J. (2011). Chemokine-GAG interactions and immune cell migration. In Chemical and Physical Biology Program Retreat. Nashville, TN: Vanderbilt University.

Chen, H., Ji, F., Olman, V., Mobley, C. K., Liu, Y., Zhou, Y., . . . Xu, Y. (2011). Optimal mutation sites for PRE data collection and membrane protein structure prediction. Structure, 19(4), 484-95. doi:10.1061/j.str.2011.02.002

Chen, H., Ji, F., Olman, V., Mobley, C. K., Liu, Y., Zhou, Y., . . . Xu, Y. (2011). Optimal Mutation Sites for PRE Data Collection and Membrane Protein Structure Prediction. STRUCTURE, 19(4), 484-495. doi:10.1016/j.str.2011.02.002

Park, Y., Pomin, V., & Prestegard, J. (2011). Structural studies of the human TSG-6 link module and chondroitin sulfate interaction by NMR. In 52nd Annual Experimental NMR Conference. Asilomar, CA: ENC.

Prestegard, J. H., & Barb, A. W. (2011). Accessibility and dynamics of immunoglobulin glycans. Retrieved from http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000291982802375&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=bccb20a1f2d949998a887c45eb30dd98

Prestegard, J. (2011). NMR characterization of glycosaminoglycans and their interaction with proteins. In Anselme Payen Award Symposium. Anaheim, CA: American Chemical Society.

Lee, H., & Prestegard, J. (2011). RDCs and RCSAs for validation of x-ray NMR structures. In Northeast Structural Genomics Retreat. New Brunswick, NJ: Rutgers University.

Pomin, V., Huang, R., Park, Y., Heiss, C., Azadi, P., Prestegard, J., & NULL, N. (2011). Specificity in enzymatic digestion of chondroitin sulfates: production of well-defined oligomers. In Georgia Glycoscience Symposium. Athens, GA: University of Georgia.

Park, Y., Pomin, V., & Prestegard, J. (2011). Structural studies of the human TSG-6 link module and chondroitin sulfate interaction by NMR. In Georgia Glycoscience Symposium. Athens, GA: University of Georgia.

Wang, X., Watson, C., Sharp, J., & Prestegard, J. (2011). Self-oligomerization of the chemokine CCL5 and its interactions with chondroitin sulfate oligomers. In Keystone Symposium on Immunity and Glycobiology. Lake Louise, Alberta, Canada: Keystone Symposia.

Barb, A., & Prestegard, J. (2011). NMR analysis demonstrates the immunoglobulin G N-glycans are accessible and dynamic. In Keystone Symposium on Immunity and Glycobiology. Lake Louise, Alberta, Canada: Keystone Symposia.

Barb, A., & Prestegard, J. (2011). NMR Analysis demonstrates the immunoglobulin G N-glycans are accessible and dynamic. In Georgia Glycoscience Symposium. Athens, GA: University of Georgia.

Barb, A., Hekmatyar, S., Prestegard, J., & Glushka, J. (2011). Enhanced NMR sensitivity for metabolic pathway investigations. In Georgia Glycoscience Symposium. Athens, GA: University of Georgia.

Prestegard, J. (2011). Monitoring glycosaminoglycan synthesis with NMR: research resources at UGA. In Cancer Imaging Lecture Series. Atlanta, GA: Winship Cancer Institute.

Ramelot, T. A., Smola, M. J., Lee, H. -W., Ciccosanti, C., Hamilton, K., Acton, T. B., . . . Kennedy, M. A. (2011). Solution Structure of 4 '-Phosphopantetheine-GmACP3 from Geobacter metallireducens: A Specialized Acyl Carrier Protein with Atypical Structural Features and a Putative Role in Lipopolysaccharide Biosynthesis. BIOCHEMISTRY, 50(9), 1442-1453. doi:10.1021/bi101932s

Prestegard, J. (2011). Integrating NMR with other technologies: high order assemblies of chemokines and glycosaminoglycans. In Bio-NMR and East-NMR Annual Users Meeting. Brno, Czech Republic: Bio-NMR and East-NMR.

Barb, A. W., & Prestegard, J. H. (2011). NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic. NATURE CHEMICAL BIOLOGY, 7(3), 147-153. doi:10.1038/NCHEMBIO.511

Barb, A. W., Cort, J. R., Seetharaman, J., Lew, S., Lee, H. -W., Acton, T., . . . Prestegard, J. H. (2011). Structures of domains I and IV from YbbR are representative of a widely distributed protein family. PROTEIN SCIENCE, 20(2), 396-405. doi:10.1002/pro.571

Barb, A. W., Glushka, J. N., & Prestegard, J. H. (2011). Kinetics of Neuraminidase Action on Glycoproteins by One- and Two-Dimensional NMR. JOURNAL OF CHEMICAL EDUCATION, 88(1), 95-97. doi:10.1021/ed900054b

Jiang, Y., McKinnon, T., Varatharajan, J., Glushka, J., Prestegard, J. H., Sornborger, A. T., . . . Bar-Peled, M. (2010). Time-Resolved NMR: Extracting the Topology of Complex Enzyme Networks. BIOPHYSICAL JOURNAL, 99(7), 2318-2326. doi:10.1016/j.bpj.2010.08.014

Varki, A., Cummings, R. D., Aebi, M., Packer, N. H., Seeberger, P. H., Esko, J. D., . . . Kornfeld, S. (n.d.). Symbol nomenclature for graphical representations of glycans. Unknown Journal, 25, 1323-1324.

Hoenig, M., Jordan, E. T., Glushka, J., Kley, S., Patil, A., Waldron, M., . . . Olson, D. E. (2011). Effect of macronutrients, age, and obesity on 6- and 24-h postprandial glucose metabolism in cats. Unknown Journal, 301, R1798-R1807. doi:10.1152/ajpregu.00342.2011

Barb, A. W., Brady, E. K., & Prestegard, J. H. (2009). Branch-Specific Sialylation of IgG-Fc Glycans by ST6Gal-I. Unknown Journal, 48, 9705-9707. doi:10.1021/bi901430h

2010

Lee, H. W. ; Wylie, G. ; Bansal, S. ; Wang, X. ; Barb, A. W. ; Macnaughtan, M. A. ; Ertekin, A. ; Montelione, G. T. ; Prestegard, J. H. Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping. Protein Science 2010, 19, 1673-1685.

Jiang, Y. ; McKinnon, T. ; Varatharajan, J. ; Glushka, J. ; Prestegard, J. H. ; Sornborger, A. T. ; Schuttler, H. B. ; Bar-Peled, M. Time-Resolved NMR: Extracting the Topology of Complex Enzyme Networks. Biophysical Journal 2010, 99, 2318-2326.

Pomin, V. H. ; Sharp, J. S. ; Li, X. Y. ; Wang, L. C. ; Prestegard, J. H. Characterization of Glycosaminoglycans by N-15 NMR Spectroscopy and in Vivo Isotopic Labeling. Analytical Chemistry 2010, 82, 4078-4088.

Shapira, B. ; Prestegard, J. H. Electron-nuclear interactions as probes of domain motion in proteins. Journal of Chemical Physics 2010, 132.

Liu, Y. Z. ; Kahn, R. A. ; Prestegard, J. H. Dynamic structure of membrane-anchored Arf center dot GTP. Nature Structural & Molecular Biology 2010, 17, 876-U128.

Raman, S. ; Lange, O. F. ; Rossi, P. ; Tyka, M. ; Wang, X. ; Aramini, J. ; Liu, G. H. ; Ramelot, T. A. ; Eletsky, A. ; Szyperski, T. ; Kennedy, M. A. ; Prestegard, J. ; Montelione, G. T. ; Baker, D. NMR Structure Determination for Larger Proteins Using Backbone-Only Data. Science 2010, 327, 1014-1018.

Liu, Y. Z. ; Prestegard, J. H. A device for the measurement of residual chemical shift anisotropy and residual dipolar coupling in soluble and membrane-associated proteins. Journal of Biomolecular Nmr 2010, 47, 249-258.

2009

Liu, Y. Z. ; Prestegard, J. H. Measurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments. Journal of Magnetic Resonance 2009, 200, 109-118.

Barb, A. W. ; Brady, E. K. ; Prestegard, J. H. Branch-Specific Sialylation of IgG-Fc Glycans by ST6Gal-I. Biochemistry 2009, 48, 9705-9707.

Liu, Y. Z. ; Kahn, R. A. ; Prestegard, J. H. Structure and Membrane Interaction of Myristoylated ARF1. Structure 2009, 17, 79-87.

DeMarco, M. L. ; Woods, R. J. ; Prestegard, J. H. ; Tian, F. Presentation of Membrane-Anchored Glycosphingolipids Determined from Molecular Dynamics Simulations and NMR Paramagnetic Relaxation Rate Enhancement. Journal of the American Chemical Society 2009, 132, 1334-1338.

Liu, S. ; Meng, L. ; Moremen, K. W. ; Prestegard, J. H. Nuclear Magnetic Resonance Structural Characterization of Substrates Bound to the alpha-2,6-Sialyltransferase, ST6Gal-I. Biochemistry 2009, 48, 11211-11219.

Kley, S. ; Hoenig, M. ; Glushka, J. ; Jin, E. S. ; Burgess, S. C. ; Waldron, M. ; Jordan, E. T. ; Prestegard, J. H. ; Ferguson, D. C. ; Wu, S. X. ; Olson, D. E. The impact of obesity, sex, and diet on hepatic glucose production in cats. American Journal of Physiology-Regulatory Integrative and Comparative Physiology 2009, 296, R936-R943.

Nkari, W. K. ; Prestegard, J. H. NMR Resonance Assignments of Sparsely Labeled Proteins: Amide Proton Exchange Correlations in Native and Denatured States. Journal of the American Chemical Society 2009, 131, 5344-5349.

2008

Macnaughtan, M. A. ; Tian, F. ; Liu, S. ; Meng, L. ; Park, S. ; Azadi, P. ; Moremen, K. W. ; Prestegard, J. H. C-13-sialic acid labeling of glycans on glycoproteins using ST6Gal-I. Journal of the American Chemical Society 2008, 130, 11864-11865.

Beel, A. J. ; Mobley, C. K. ; Kim, H. J. ; Tian, F. ; Hadziselimovic, A. ; Jap, B. ; Prestegard, J. H. ; Sanders, C. R. Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): Does APP function as a cholesterol sensor?. Biochemistry 2008, 47, 9428-9446.

Wang, X. ; Bansal, S. ; Jiang, M. ; Prestegard, J. H. RDC-assisted modeling of symmetric protein homo-oligomers. Protein Science 2008, 17, 899-907.

Bansal, S. ; Miao, X. ; Adams, M. W. W. ; Prestegard, J. H. ; Valafar, H. Rapid classification of protein structure models using unassigned backbone RDCs and probability density profile analysis (PDPA). Journal of Magnetic Resonance 2008, 192, 60-68.

Zheng, S. L. ; Kaur, G. ; Wang, H. C. ; Li, M. Y. ; Macnaughtan, M. ; Yang, X. C. ; Reid, S. ; Prestegard, J. ; Wang, B. H. ; Ke, H. M. Design, Synthesis, and Structure-Activity Relationship, Molecular Modeling, and NMR Studies of a Series of Phenyl Alkyl Ketones as Highly Potent and Selective Phosphodiesterase-4 Inhibitors. Journal of Medicinal Chemistry 2008, 51, 7673-7688.

Prestegard, J. H. ; Yu, F. PHYS 167-Glycosaminoglycans: Structure and interaction using sparse isotopic labels. Abstracts of Papers of the American Chemical Society 2008, 236, 167-PHYS.

Bryson, M. ; Tian, F. ; Prestegard, J. H. ; Valafar, H. REDCRAFT: A tool for simultaneous characterization of protein backbone structure and motion from RDC data. Journal of Magnetic Resonance 2008, 191, 322-334.

Liu, S. ; Prestegard, J. H. CARB 122-Mapping sialyltransferase active sites using isotopically labeled and spin-labeled NMR probes. Abstracts of Papers of the American Chemical Society 2008, 235, 122-CARB.

Yu, F. ; Wang, X. ; Adams, A. ; Prestegard, J. H. ANYL 91-NMR Structural investigation of chondroitin sulfate oligomer complexed to RANTES. Abstracts of Papers of the American Chemical Society 2008, 235, 91-ANYL.