Director: Asokan Anbanandam, Ph.D. (CV)
asokan@ku.edu
Telephone: 785-864-3746
Fax: 785-864-8141

The University of Kansas (map)
Structural Biology Center, Room 1011
2121 Simons Dr.
Lawrence, KS 66047

The COBRE Biomolecular NMR Laboratory maintains two high field NMR spectrometers in support of structural and dynamics studies of biomolecules with COBRE and other investigators in Kansas and the region. Its capabilities include determining high resolution structures, biological macromolecules, elucidation and structural mapping of protein-protein, protein-nucleic acid, protein-peptide, protein-drug interactions, and studies of the dynamics of proteins and their complexes in solution.

Laboratory staff provide advice, consultation, training, assistance and service to investigators. The staff is also responsible for maintenance and upgrades of the two high field NMR instruments, implementation of new NMR pulse sequences, and assisting local and remote users with technical problems.

The laboratory is equipped with a Bruker Avance 800 MHz NMR instrument fitted with a TCI cryoprobe and a Varian Innova 600 MHz with a variety of probes. It is located in close proximity to other core service laboratories in the KU Structural Biology Center.

Services offered include:
• Training for new instrument users
• Consultation on proposal preparation
• 1D-4D NMR Data Collection.
• Data processing, analysis, and interpretation.
• Structure determination.
• Heteronuclear relaxation measurements and data analysis
• H/D exchange measurements by NMR
• NMR titration measurement

Work Request Form
Fee Schedule
Ongoing Research Projects
Acknowledgement Policy
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The 800 MHz is housed in the Structural Biology Center (SBC).

The Varian Inova 600 MHz NMR, operated by the
Biomolecular NMR Laboratory staff, is in the Multidisciplinary Research Building on the KU West Campus.

Steering Committee:
James Bann, Wichita State University
Roberto De Guzman, The University of Kansas
Jennifer Laurence, The University of Kansas
Mario Rivera, The University of Kansas

Other COBRE Core Laboratories:
COBRE Protein Production Laboratory
COBRE Protein Structure Laboratory

Other links of interest:
KU NMR Laboratory
Mass Spectrometry Laboratory
X-ray Crystallography Laboratory
Molecular Graphics and Modeling Laboratory
Analytical Proteomics Laboratory
Applied Bioinformatics Laboratory

Selected publications citing assistance provided by the COBRE BioMolecular NMR Laboratory:

Williams, A.S., Lovell, S., Anbanandam, A., El-Chami, R., Bann, J.G. Domain 4 of the anthrax protective antigen maintains structure and binding to the host receptor CMG2 at low pH. Protein Sci. 2009, 18: 2277-2286.

Wang Y, Zhang L, Picking WL, Picking WD, De Guzman RN. Structural dissection of the extracellular moieties of the type III secretion apparatus. Mol. BioSyst. 4, 1176-80, 2008.

Wang Y, Boudreaux DM, Estrada DF, Egan CW, St. Jeor SC, De Guzman RN. NMR structure of the N-terminal coiled coil domain of the Andes hantavirus nucleocapsid protein. J. Biol. Chem. 283, 28297-304, 2008. PMID: 18687679.

Nonoyama, A., Laurence, J.S., Garriques, L., Qi, H., Le, T., and Middaugh, C.R., ³A biophysical characterization of AC137 and evaluation of the empirical phase diagram using a peptide model,² J. Pharm. Sci., 97:2552-67 (2008).

Martin, A., David. V., Laurence, J.S., Schwarz, P.M., Lafer, E.M., Hedge, A.M., and Rowe, P.S., ³Degradation of MEPE, DMP1 & release of SIBLING ASARM-peptides (minhibins): ASARM-peptide(s) are directly responsible for defective mineralization in HYP², Endocrinology 149: 1757-1772, 2008.

Skinner, A.L. and Laurence, J.S., ³High-field Solution NMR Spectroscopy as a tool for Assessing Protein Interactions with Small Molecule Ligands², J. Pharm. Sci. 97: 4670-4695, 2008.

Ciaccio, N.A., Moreno, M.L., Bauer, R.L. and Laurence, J.S., ³High-Yield Expression in E. coli and Refolding of the bZIP Domain of Activating Transcription Factor 5², Protein Expr. Purif. 62, 235-243, 2008.

Wang, Y, Ouellette, AN, Egan, CW, Rathinavelan, T, Im, W, and De Guzman, RN. Differences in the electrostatic surfaces of the type III secretion needle proteins PrgI, BsaL, and MxiH. J. Mol. Biol. 371, 1304-14, 2007.

Zhang L, Wang Y, Olive AJ, Smith ND, Picking WD, De Guzman RN, Picking WL. Identification of the MxiH needle protein residues responsible for anchoring IpaD to the type III secretion needle tip. J. Biol. Chem. 282, 32144-32151, 2007.

Zhang, L, Wang, Yu, Picking, WL, Picking, WD, De Guzman, RN. Solution Structure of Monomeric BsaL, the Type III Secretion Needle Protein of Burkholderia pseudomallei. J. Mol. Biol. 359, 322-330, 2006.

COBRE in Protein Structure and Function