Applying nuclear magnetic resonance spectroscopy in the study of biologically important macromolecular assemblies

E-mail: jpresteg@ccrc.uga.edu
Telephone: 706-542-6281
Fax: 706-542-4412

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Dr. Prestegard's group is applying nuclear magnetic resonance (NMR) spectroscopy to the study of the structure and function of biologically important macromolecular assemblies involving carbohydrates, proteins, and membranes. Research in the Prestegard laboratory focuses on NMR methods development, membrane proteins, cell-surface carbohydrates, protein structure, and protein-protein interactions.

Proteins are large molecules that are targets (receptors) of natural ligands (smaller molecules that bind specifically to the active site of a protein) as well as pharmaceuticals. An essential part of developing any new drug is to determine how that drug will bind to its target protein(s) and to characterize the structures and conformations of the interacting molecules, a particularly difficult task when flexible structures such as carbohydrates are involved. 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. However, progress has been impeded by reliance on short-range interactions (known as NOEs) that are limited in their ability to characterize the relative placement of remote parts of macromolecules or to characterize the average conformation of flexible ligands. These limitations are particularly severe in recognition of carbohydrate-containing ligands because they are inherently flexible and because the proteins that recognize them often function as multimers of loosely connected domains.

The Prestegard group has recently made some important advances in developing non-NOE-based structure determination methods. These methods rely on a more direct NMR measurement that can be made in "ordered" media, in the presence of high magnetic fields. Using these new methods the Prestegard group has succeeded in characterizing the relative orientation of two domains in a carbohydrate-binding protein and in collecting structural data on a flexible trisaccharide (a molecule composed of three sugars) without the use of NOEs. The experiments provide data in a fraction of the time required by the traditional NOE-based approach and can provide a unique structural perspective on which to base the design of new drugs.

NMR methods development. Methods development is closely related to the demands of the applications. For example, some exciting diffusion-edited amide exchange experiments have been developed for the investigation of the energetics and kinetics of protons involved in hydrogen bonds. Hydrogen bonding is important in stabilizing protein structural elements and in protein-carbohydrate recognition, both subjects being studied in the Prestegard group. Neural network-based automated assignment programs for multi-dimensional NMR spectra have been developed, as have statistics-based spectral analysis programs. These programs are essential in achieving less tedious and more precise NMR-based structural analysis.

An ongoing objective of the Prestegard group is to extract new types of information from NMR and related experiments. Current projects involve the use of residual dipolar couplings that occur in molecules oriented by very high magnetic fields and cross-correlation effects that involve chemical shift anisotropies that also become large in high fields. Both topics rely on the design of new experiments and in-depth theoretical analysis of experimental results.

Membrane proteins. The structural analysis of membrane proteins is one of the major challenges in biophysical chemistry today. It is a major challenge because these proteins prefer an environment that is neither crystal nor solution. Unfortunately, crystal and solution phases are the only two phases for which structure determination methods are well established. The Prestegard lab has undertaken the development of NMR-based structure determination methods that are applicable in a medium that mimics the partial, liquid crytalline order of natural membranes. These methods are currently being applied to peptides that present typical membrane protein structural motifs, such as trans bilayer helices and surface-associated amphipathic helices.

Cell-surface carbohydrates. Carbohydrates covalently linked to proteins (glycoproteins) and to lipids (glycolipids) are also present on the surfaces of membranes. In fact, they are the primary mediators in processes that involve interaction of a cell with its external environment. This external environment includes important processes such as cell-cell interactions, hormone stimulation, and invasion by pathogens. Structural characterization of the carbohydrate moieties in their nature environment is essential to understanding and controlling the processes in which they are involved. Many of the NMR methods being developed to characterize membrane proteins are equally applicable to cell-surface carbohydrates. In addition, methods that are more focused on the details of protein-carbohydrate recognition interactions are important. A number of lectins from plant and animal sources are being studied as models for these recognition processes and as a testing ground for methods that can characterize them.

Protein structure and protein-protein interactions. Knowledge of protein structure is essential to understanding a very large number of biochemical processes. However, proteins seldom act alone. They interact with substrates, receptors, and one another to fine tune their activities and specificities. NMR spectroscopy offers the opportunity not only to determine protein structure (in solution, for the cases of interest to the Prestegard group) but to focus on particular regions involved in critical contacts. Isotope-edited NMR experiments are a key component enabling analyses of these special regions. The Prestegard group has implemented a full array of these experiments and is applying them to interesting protein systems. One study involves components of chaperonin systems important to protein folding. Another involves components of multi-enzyme systems important in the synthesis and modification of long chain fatty acids.

Dr. Prestegard's research is supported by the National Science Foundation, the National Institutes of Health, and the Georgia Research Alliance.

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Journal Articles
Book Chapters are listed at the bottom of this page.

W.K. Nkari, J.H. Prestegard. 2009. NMR resonance assignments of sparsely labeled proteins: amide proton exchange correlations in native and denatured states. J. Am. Chem. Soc. 131: 5344-5349. PMID:19317468

G.T. Montelione, C. Arrowsmith, M.E. Girvin, M.A. Kennedy, J.L. Markley, R. Powers, J.H. Prestegard, T. Szyperski. 2009. Unique opportunities for NMR methods in structural genomics. J. Struct. Funct. Genomics 10: 101-106. PMID:19288278

M. Bryson, F. Tian, J.H. Prestegard, H. Valafar. 2008. REDCRAFT: A tool for simultaneous characterization of protein backbone structure and motion from RDC data. J. Magnetic Resonance 191: 322-234. PMID:18258464

S. Bansal, X. Miao, M.W.W. Adams, J.H. Prestegard, H. Valafar. 2008. Rapid classification of protein structure models using unassigned backbone RDCs and probability density profile analysis. J. Magnetic Resonance 192: 60-68. PMID:18321742

X. Wang, S. Bansal, M. Jiang, J.H. Prestegard. 2008. RDC assisted modeling of symmetric protein homo-oligomers. Protein Science 17: 899-907. PMID:18436958

T. Zhuang, H.-S. Lee, B. Imperiali, J.H. Prestegard. 2008. Structure determination of a Galectin-3-carbohydrate complex using paramagnetism-based NMR constraints. Protein Science 17: 1220-1231. PMID:18413860

Y. Liu, J.H. Prestegard. 2008. Direct measurement of dipole-dipole/CSA cross-correlated relaxation by a constrant-time experiment. J. Magnetic Resonance 193: 23-31. PMID:18406649

M.A. Macnaughtan, F. Tian, S. Liu, L. Meng, S. Park, P. Azadi, K.W. Moremen, J.H. Prestegard. 2008. 13C-cialic acid labeling of glycans on glycoproteins using ST6Gal-1. J. Am Chem. Socl 130: 11864-11865. PMID:18700760

X. Wang, T. Weldeghorghis, G. Zhang, B. Imperiali, J.H. Prestegard. 2008. Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase. Proteins: Structure, Function & Genetics 16: 965-975. PMID:18547528

Y. Liu, R.A. Kahn, J.H. Prestegard. 2008. Structure and membrane intraction of myristoylated ARF1. Structure. 17: 79-87. PMID:19141284

S. Zheng, G. Kaur, H. Wang, M.A. Hollingsworth, M. Macnaughtan, X. Yang, J.S.G. Reid, J.H. Prestegard, B.C. Wang, L.H. Keller. 2008. Design, synthesis, and structure-activity relationship, molecular modeling and NMR studies of a series of phenylalkyl ketones as highly potent and selective phosphodiesterase-4 inhibitors. J. Med. Chem. 51: 7673-7688.

D. Parish, J. Benach, G. Liu, K.K. Singarapu, R. Xiao, T. Acton, M. Su, S. Bansal, J.H. Prestegard, J. Hunt, G. Montelione, T. Szyperski. 2008. Protein chaperones Q8ZP25_SALTY from Salmonella typhimurium and HYAE_ECOLI from Escherichia coli exhibit thioredoxin-like structures despite lack of canonical thioredoxin active site sequence motif. J. Struct. Funct. Genomics 9: 41-49. PMID:19039680

L. Feng, H.S. Lee, J.H. Prestegard. 2007. NMR resonance assignments for sparsely 15N labeled proteins. J. Biomol. NMR 38: 213-219. PMID:17487550

S. Liu, A. Venot, L. Meng, F. Tian, K.W. Moremen, G.J. Boons, J.H. Prestegard. 2007. Spin-labeled analogs of CMP-NeuAc as NMR probes of the alpha-2-6-sialyltransferase ST6Gal I. Curr. Opinion Chem. Biol. 14: 409-418. PMID:17462576

X. Wang, H.S. Lee, F.J. Sugar, F.E. Jenney,, M.W. Adams, J.H. Prestegard. 2007. PF0610, a novel winged HTH variant possessing a rubredoxin-like Zn ribbon motif from the hyperthermophilic archaeon, Pyrococcus furiosus. Biochemistry 46: 752-761. PMID:17223696

R.D. Seidel,, T. Zhuang, J.H. Prestegard. 2007. Bound-state residual dipolar couplings for rapidly exchanging ligands of His-tagged proteins. J. Am. Chem. Soc. 129: 4834-4839. PMID:17385862

M.S. Macnaughtan, M. Kamar, G. Alvarez-Manilla, A. Vernot, J. Glushka, J.M. Pierce, J.H. Prestegard. 2007. NMR structural chaacterization of substrates bound to N-acetylglucosaminyltranferase V. J. Mol. Biol. 366: 1266-1281. PMID:17204285

S.C. Sahu, V. Simplaceanu, Q. Gong, N.T. Ho, F. Tian, J.H. Prestegard, C. Ho. 2007. Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector. Biochemistry 46: 9973-9980. PMID:17691822

X. Wang, S. Srisailam, A.A. Yee, A. Lemak, C. Arrowsmith, J.H. Prestegard, F. Tian. 2007. Domain-domain motions in proteins from time-modulated psudocontact shifts. J. Biomol. NMR 39: 53-61. PMID:17657568

F. Yu, J.J. Wolff, I.J. Amster, J.H. Prestegard. 2007. Conformational preferences of chondroitin sulfate oligomers using partially oriented NMR spectroscopy of 13C-labeled acetyl groups. J Am Chem Soc 129: 13288-13297. PMID:17924631

T. Zhuang, H. Leffler, J.H. Prestegard. 2006. Enhancement of Bound-State Residual Dipolar Couplings: Conformational Analysis of Lactose Bound to Galectin-3. Protein Sci. 15: 1780-1790. PMID:16751604

S.C. Sahu, V. Simplaceanu, Q. Gopng, N.T. Ho, J.G. Glushka, J.H. Prestegard, SIZE=8 Chien. 2006. Orientation of Deosyhemoglobin at High Magnetic Fields: Structural Insights from RDCs in Solution. J. Am. Chem. Soc. 128: 6290-6291. PMID:16683773

L. Feng, R. Orlando, J.H. Prestegard. 2006. Amide proton back-exchange in deuterated peptides: Applications to MS and NMR analyses. J. Anal. Chem 78: 6885-6892. PMID:17007511

K.L. Mayer, Y Qu, S. Bansal, P.D. LeBlond, F.E. Jenney, Jr., P.S. Brereton, M.W. Adams, Y. Xu, J.H. Prestegard. 2006. Structure determination of a new protein from backbone-centered NMR data and NMR-assisted structure prediction. Proteins: Structure, Function & Genetics 65: 480-489. PMID:16927360

F. Yu, J.H. Prestegard. 2006. Structural monitoring of oligosaccharides through 13C enrichment and NMR observation of acetyl groups. Biophys. J. 91: 1952-1959. PMID:16782783

J. Wang, H. Valafar, J.H. Prestegard. 2005. Assessment of protein alignment using ¹H-¹H residual dipolar couplings measurements. J. Magn. Reson. 172: 85-90. PMID:15589411

H. Valafar, K.L. Mayer, C.M. Bougault, P.D. LeBlond, F.E. Jenner, P.S. Bereton, M.W.W. Adams, J.H. Prestegard. 2005. Backbone solution structures of proteins using residual dipolar couplings: application to a novel structure genomics target. J. Struct. Funct. Genomics 5: 241-254.

M. Macnaughtan, A.M. Kane, J.H. Prestegard. 2005. Mass spectrometry assisted assignment of NMR resonances in reductively ¹³C-methylated proteins. J. Am. Chem. Soc. 127: 17626-17627. PMID:16351091

A.I. Kishore, M.R. Mayer, J.H. Prestegard. 2005. Partial ¹³C Isotopic Enrichment of Nucleoside Monophosphates: Useful Reporters for NMR Structural Studies. Nuc. Acids. Res. 33: Art. No. E164-. PMID:16254075

K.L. Mayer, Y. Qu, S. Bansal, P.D. LeBlond, F.E. Jenney%2C, P.S. Brereton, M.W.W. Adams, Y. Xu, J.H. Prestegard. 2005. Structure of a Novel Protein from Backbone-Centered NMR Data and NMR-Assisted Structure Prediction. Proteins: Structure, Function, and Bioinformatics In press.

J.H. Prestegard, K.L. Mayer, H. Valafar, G.C. Benison. 2005. Determination of protein backbone structures from residual dipolar couplings. Methods Enzymol. 394: 175-209. PMID:15808221

L. Feng, R. Orlando, J.H. Prestegard. 2004. Mass spectrometry assisted assignment of NMR resonances in ¹⁵N labeled proteins. J. Am. Chem. Soc. 126: 14377-14379. PMID:15521756

L.C. Morris, H. Valafar, J.H. Prestegard. 2004. Assignment of protein backbone resonances using connectivity, torsion angles and ¹³Ca chemical shifts. J. Biomol. NMR 29: 1-9. PMID:15017135

C. Bougault, L. Feng, J. Glushka, E. Kupce, J.H. Prestegard. 2004. Quantitation of rapid proton-deuteron amide exchange using hadamard spectroscopy. J. Biomol. NMR 28: 385-390. PMID:14872129

H. Valafar, J.H. Prestegard. 2004. REDCAT: A residual dipolar coupling analysis tool. J. Mag. Res. 167: 228-241. PMID:15040978

P.J.A. Erbel, R.D. Seidel, S.E. Macintosh, L.N. Gentile, J.C. Amor, R.A. Kahn, J.H. Prestegard, L.P. McIntosh, K.A. Gardner. 2004. Cyclic enterobacterial common antigen: potential contaminant of bacterially-expressed protein preparations. J. Biomol. NMR 29: 199-204. PMID:15014233

J.H. Prestegard, C.M. Bougault, A.I. Kishore. 2004. Residual dipolar couplings in structure determination of biomolecules. Chem. Rev. 104: 3519-3540. PMID:15303825

R.D. Seidel, J.C. Amor, R.A. Kahn, J.H. Prestegard. 2004. Conformational changes in human Arf1 on nucleotide exchange and deletion of membrane binding elements. J. Biol. Chem. 279: 48307-48318. PMID:15308674

N.U. Jain, T.J.O. Wyckoff, C.R.H. Raetz, J.H. Prestegard. 2004. Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: the 95 Kda complex of LpxA with acyl carrier protein. J. Mol. Biol. 343: 1379-1389. PMID:15491619

R.D. Seidel, J.C. Amor, R.A. Kahn, J.H. Prestegard. 2004. Structural perturbations in human ADP ribosylation factor-1 accompanying the binding of phosphatidylinositides. Biochemistry 172: 85-90. PMID:15581351

X. Yi, A. Venot, J. Glushka, J.H. Prestegard. 2004. Glycosidic torsional motions in a bicelle-associated disaccharide from residual dipolar couplings. J. Am. Chem. Soc. 126: 13636-13638. PMID:15493919

H. Valafar, K.L. Mayer, C.M. Bougault, P.D. LeBlond, F.E. Jenney, Jr., P.S. Brereton, M.W. Adams, J.H. Prestegard. 2004. Backbone solution structures of proteins using residual dipolar couplings: application to a novel structural genomics target. J Struct Funct Genomics 5: 241-254. PMID:15704012

C. Bougault, M.K. Eidsness, J.H. Prestegard. 2003. Hydrogen Bonds in rubredoxins from mesophilic and hyperthermophilic organisms. Biochemistry 42: 4357-4372. PMID:12693931

J.N. Glushka, M. Terrell, W.S. York, M.A. O'Neill, A. Gucwa, A.G. Darvill, P. Albersheim, J.H. Prestegard. 2003. Primary structure of the 2-O-methyl-a-L-fucose-containing side chain of the pectic polysaccharide, rhamnogalacturonan II. Carbohydr. Res. 338: 341-352. PMID:12559732

N. Jain, S. Noble, J.H. Prestegard. 2003. Structural characterization of a mannose binding protein-trimannoside complex using residual dipolar couplings. J. Mol. Biol. 328: 451-462. PMID:12691753

K. Umemoto, H. Leffler, A. Venot, H. Valafar, J.H. Prestegard. 2003. Conformational differences in liganded and unliganded states of Galectin-3. Biochemistry 42: 3688-3695. PMID:12667058

H. Valafar, J.H. Prestegard. 2003. Rapid classification to a protein fold family using a statistical anaylsis of dipolar couplings. Bioinformatics 19: 1549-1555. PMID:12912836

J.C. Amor, R.D. Seidel, F. Tian, R.A. Kahn, J.H. Prestegard. 2002. ¹H, ¹⁵, and ¹³C assignments of full length ADP ribosylation factor using triple resonance connectivities and dipolar couplings. J. Biomol. NMR 23: 253-254.

E.W. Sayers, J.H. Prestegard. 2002. Conformation of a trimannoside bound to mannose-binding protein by NMR and MD simulations. Biophys J. 82: 2683-2399. PMID:11964255

A.H. Siriwardena, F. Tian, S. Noble, J.H. Prestegard. 2002. A straightforward NMR-spectroscopy-based method for rapid library screening.. Angew. Chem. Int. Engl. 41: 3454-3457. PMID:12298062

H. Valafar, J.H. Prestegard, F. Valafar. 2002. Datamining protein structure databanks for cyrstallization pattern of proteins. Ann. N.Y. Acad. Sci. 980: 13-23. PMID:12594078

E.R. Zartler, F.E. Jenney, F.E. Jenney%2C, M. Terrell, M.K. Eidsness, M.W.W. Adams, J.H. Prestegard. 2001. Structural basis for thermostability in aporubredoxins from Pyrococcus furiosus and Clostridium pasteurianum. Biochemistry 40: 7279-7290. PMID:11401576

N.U. Jain, A. Venot, K. Umemoto, H. Leffler, J.H. Prestegard. 2001. Distance mapping of protein-binding sites using spin labeled oligosaccharide ligands. Protein Sci. 10: 2393-2400. PMID:11604544

J.H. Prestegard, A.I. Kishore. 2001. Partial alignment of biomolecules: An aid to NMR characterization. Curr. Opinion Chem. Biol. 5: 584-590. PMID:11578934

F. Tian, H. Valafar, J.H. Prestegard. 2001. A dipolar coupling based strategy for simultaneous resonance assignment and structure determination of protein backbones. J Am Chem Soc 123: 11791-11796. PMID:11716736

J.H. Prestegard, H. Valafar, J. Glushka, F. Tian. 2001. Nuclear magnetic resonance in the era of structural genomics. Biochemistry 40: 8677-8685. PMID:11467927

J.R. Tolman, H.M. Al-Hashimi, L.E. Kay, J.H. Prestegard. 2001. Structural and dynamic analysis of residual dipolar coupling data for proteins. J Am Chem Soc 123: 1416-1424. PMID:11456715

F. Tian, H.M. Al-Hashimi, J.L. Craighead, J.H. Prestegard. 2001. Conformational analysis of a flexible oligosacchardie using residual dipolar couplings. J Am Chem Soc 123: 485-492. PMID:11456551

H.M. Al-Hashimi, P.J. Bolon, J.H. Prestegard. 2000. Molecular symmetry as an aid to geometry determination in ligand protein complexes. J. Magn. Reson. 142: 153-158. PMID:10617446

H.M. Al-Hashimi, H. Valafar, M. Terrell, E.R. Zartler, M.K. Eidsness, J.H. Prestegard. 2000. Variation of molecular alignment as a means of resolving orientational ambiguities in protein structures from dipolar couplings. J. Magn. Reson. 143: 402-406. PMID:10729267

J.A. Losonczi, F. Tian, J.H. Prestegard. 2000. Nuclear magnetic resonance studies of the N-terminal fragment of adenosine dipyhosphate ribosylation factor 1 in micelles and bicelles: Influence of N-myristoylation. Biochemistry 39: 3804-3816. PMID:10736181

J.H. Prestegard, H.M. Al-Hashimi, J.R. Tolman. 2000. NMR structures of biomolecules using field oriented media and residual dipolar couplings. Q. Rev. Biophys. 33: 371-424. PMID:11233409

F. Tian, C.A. Fowler, E.R. Zartler, A. Jenney, M.W. Adams, J.H. Prestegard. 2000. Direct measurement of ¹H-¹H dipolar couplings in proteins: a complement to traditional NOE measurements. J. Biomol. NMR. 18: 23-31. PMID:11061225

C.A. Fowler, F. Tian, H.M. Al-Hashimi, J.H. Prestegard. 2000. Rapid determination of protein folds using residual dipolar couplings. J. Mol. Biol. 304: 447-460. PMID:11090286

E.W. Sayers, J.H. Prestegard. 2000. Solution conformations of a trimannoside from nuclear magnetic resonance and molecular dynamics simulations. Biophys. J. 79: 3313-3329. PMID:11106634

F. Tian, H.M. Al-Hashimi, J. Craighead, J.H. Prestegard. 2000. Conformational analysis of a flexible oligosaccharide using residual dipolar couplings. J. Am. Chem. Soc. 123: 485-492.

J.R. Tolman, H.M. Al-Hashimi, L.E. Kay, J.H. Prestegard. 2000. Structural and dynamic analysis of residual dipolar coupling data for proteins. J. Am. Chem. Soc. 123: 1416-1424.

M.W.F. Fischer, J. Losonczi, J.L. Weaver, J.H. Prestegard. 1999. Domain orientation and dynamics in multidomain proteins from residual dipolar couplings. Biochemistry 38: 9013-9022.

K. Huang, J.M. Flanagan, J.H. Prestegard. 1999. The influence of C-terminal extension on the structure of the "J-domain" in E. coli DnaJ. Protein Sci. 8: 203-214.

K. Huang, R. Ghose, J.M. Flanagan, J.H. Prestegard. 1999. Backbone dynamics of the N-terminal domain in E. coli DnaJ determined by 15N and 13CO-relaxation measurements. Biochemistry 38: 10567-10577.

J.A. Losonczi, M. Andrec, M.W.F. Fischer, J.H. Prestegard. 1999. Order matrix analysis of residual dipolar couplings using singular value decomposition. J. Magn. Reson. 138: 334-342.

B.A. Salvatore, J.H. Prestegard. 1999. Synthesis of a ¹⁵N, ¹³C-labeled lactam analog of a G_M4-lactone cell-surface glycolipid. Tetrahedron Lett. 39: 9319-9322.

F. Tian, P.J. Bolon, J.H. Prestegard. 1999. Intensity based measurement of homonuclear residual dipolar couplings from CT-COSY. J. Am. Chem. Soc. 121: 7712-7713.

P.J. Bolon, H.M. Al-Hashimi, J.H. Prestegard. 1999. Residual dipolar coupling derived orientational constraints on geometry in a 53 kDA protein-ligand complex. J. Mol. Biol. 293: 107-115.

F. Tian, J.A. Losonczi, M.W.F. Fischer, J.H. Prestegard. 1999. Sign determination of dipolar couplings in field-oriented bicelles by variable angle sample spinning (VASS). J. Biomol. NMR 15: 145-150.

M. Andrec, J.H. Prestegard. 1998. A Metropolis Monte Carlo implementation of Bayesian time-domain parameter estimation: application to coupling constant estimation from antiphase multiplets. J. Magn. Reson. 130: 217-232.

P.J. Bolon, J.H. Prestegard. 1998. COSY crosspeaks from ¹H-¹H dipolar couplings in NMR spectra of field oriented oligosaccharides. J. Am. Chem. Soc. 120: 9366-9367.

R. Ghose, J.H. Prestegard. 1998. Improved estimation of CSA-dipolar coupling cross-correlation rates from laboratory-frame relaxation experiments. J. Magn. Reson. 134: 308-314.

R. Ghose, K. Huang, J.H. Prestegard. 1998. Measurement of cross-correlation between dipolar coupling and chemical shift anisotropy in the spin relaxation of 13C-,15N-labeled proteins. J. Magn. Reson. 135: 487-499.

J.A. Losonczi, J.H. Prestegard. 1998. Improved dilute bicelle solutions for high-resolution NMR of biological macro-molecules. J. Biomol. NMR 12: 447-451.

J.A. Losonczi, J.H. Prestegard. 1998. Nuclear magnetic resonance characterization of the myristoylated N-terminal fragment of ADP-ribosylation factor 1 in magnetically oriented membrane array. Biochemistry 37: 706-716.

J.H. Prestegard. 1998. New techniques in structural NMR -- anisotropic interactions. Nature, Struc. Biol., NMR Suppl. : 517-522.

E.W. Sayers, J.L. Weaver, J.H. Prestegard. 1998. Hydrogen bonding geometry of a protein-bound carbohydrate from water exchange-mediated cross-relaxation. J. Biomol. NMR 12: 209-222.

J.L. Weaver, J.H. Prestegard. 1998. Nuclear magnetic resonance structural and ligand binding studies of BLBC, a two-domain fragment of barley lectin. Biochemistry 37: 116-128.

Book Chapters

M.W.W. Adams, H. Dailey, L.J. DeLucas, M. Luo, J.H. Prestegard, J.P. Rose, B.C. Wang. 2003. The Southeast Collaboratory for Structural Genomics: A high-throughput gene to structure factory. In: Acc. Chem. Res, pp. 191-198.

J.H. Prestegard, J. Glushka. 2002. Residual dipolar couplings: Structure and Dynamics of Glycolipids. In: NMR Spectroscopy of Glyco-Conjugates, (Jimenez-Barbero and Peters, eds.), pp. 231-243.

J.H. Prestegard. 2002. High resolution NMR of biomolecules. In: High Magnetic Fields: Applications in Condensed Matter Physics and Spectroscopy, LNP Vol. 595 (C. Berthier, L.P. Levy, G. Martinez,eds.), pp. 426-434. Springer-Verlag.

J.H. Prestegard, J.R. Tolman, H.M. Al-Hashimi, M. Andrec. 1999. Protein structure and dynamics from field-induced residual dipolar couplings. In: Biological Magnetic Resonance: Structure Computation and Dynamics in Protein NMR (N.R. Krishna and L.J. Berliner, eds.), Vol.Vol. 17:311-355. Kluwer Academic-Plenum Publishers, New York..

J.H. Prestegard, P.J. Bolon, H.M. Al-Hashimi, J. Losonczi, M.W.F. Fischer. 1999. Field induced order in biomolecular solutions: A new soruce of NMR structural data. In: Proceedings of the Physical Phenomena at High Magnetic Fields-III (Z. Fisk, L.W. Gorkov, R. Schrieffer, eds.), pp. 419-420. World Scientific Publishing Co. Singapore.

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