Glycan Structure Analysis

The Alberta Glycomics Centre Glycan Structure Analysis core offers a unique set of services and expertise for solving your problems in Glycomics research. We are experienced in the analysis of complex glycans and glycoproteins. We can provide routine analysis, or help to interpret complex data. Our services include:

  • NMR
    •  Routine characterization of oligosaccharide samples for QC and analysis
    • Complex structure determination, including high-resolution conformational analysis and protein-carbohydrate complexes
    • 1D/2D NMR (300, 400, 500, 600, 700 MHz), STD-NMR
    • Compositional analysis (stoichiometry) of polysaccharides
  • Mass Spectrometry
    • Oligosaccharide/Glycan sequencing
    • Determination of unusual or modified glycan structures
    • Nano-ES, MALDI TOF/TOF, FT-ICR
  • Molecular modeling
    • Molecular dynamics of glycoproteins and protein-carbohydrate complexes
    • AMBER (GLYCAM), Gaussian
  • Biomolecular interactions
    • SPR (BIAcore), Microcalorimetry
  • Expertise
    • Glycan analysis is often complex, and can require advanced training. We will work with you to interpret data from even your most complex samples.

     

Chris CairoDr. Christopher Cairo Principal Investigator Alberta Glycomics Centre Professor of Chemistry, University of Alberta

Chris originally hails from the great state of New York, where he pursued his undergraduate degree in Chemistry at the State University of New York-Albany. In 1996, he moved on to pursue his Ph.D. at the University of Wisconsin-Madison under the supervision of Prof. Laura L. Kiessling. After completing his graduate studies in 2002, he became an NIH Postdoctoral fellow at Harvard Medical School in the Department of Biological Chemistry and Molecular Pharmacology with Prof. David E. Golan. Chris began his appointment as an Assistant Professor of Chemistry at the University of Alberta in July of 2006, and is a Principal Investigator in the Alberta Glycomics Centre, and is also a member of the Consortium for Functional Glycomics. His research interests include bioorganic and peptide chemistry, carbohydrate chemistry, chemical biology, biophysics, and cell biology.

For more information on this specific project, please contact Dr. Klay Dyer, AGC Manager at 780-248-1908 or via email at klay@ualberta.ca

Glycan and glycopeptide sequencing by MS

 

Molecular Modeling of Carbohydrate-Protein Complexes
Simulation and interpretation of high-resolution NMR data (TOP: simulated; BOTTOM: actual data)

Research Highlights

  1. Clarke, B. R., M. R. Richards, et al. (2011). “In vitro reconstruction of the chain termination reaction in biosynthesis of the Escherichia coli O9a O-polysaccharide: the chain-length regulator, WbdD, catalyzes the addition of methyl phosphate to the non-reducing terminus of the growing glycan.” Journal of Biological Chemistry 286(48): 41391-41401.
  2. Greenfield, L. K., M. R. Richards, et al. (2012). “Biosynthesis of the polymannose lipopolysaccharide O-antigens from Escherichia coli serotypes O8 and O9a requires a unique combination of single- and multiple-active site mannosyltransferases.” Journal of Biological Chemistry 287(42): 35078-35091.
  3. Greenfield, L. K., M. R. Richards, et al. (2012). “Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigens.” Journal of Biological Chemistry 287(45): 38135-38149.
  4. Loka, R. S. and C. W. Cairo (2010). “Immobilization of carbohydrate epitopes for surface plasmon resonance using the Staudinger ligation.” Carbohydrate Research 345(18): 2641-2647.
  5. Loka, R. S., C. M. Sadek, et al. (2010). “Conjugation of synthetic N-acetyl-lactosamine to azide-containing proteins using the Staudinger ligation.” Bioconjugate Chemistry 21(10): 1842-1849.
  6. Leymarie, N.; Griffin, P. J.; Jonscher, K.; Kolarich, D.; Orlando, R.; McComb, M.; Zaia, J.; Aguilan, J.; Alley, W. R.; Altmann, F.; Ball, L. E.; Basumallick, L.; Bazemore-Walker, C. R.; Behnken, H.; Blank, M. A.; Brown, K. J.; Bunz, S.-C.; Cairo, C. W.; Cipollo, J. F.; Daneshfar, R.; Desaire, H.; Drake, R. R.; Go, E. P.; Goldman, R.; Gruber, C.; Halim, A.; Hathout, Y.; Hensbergen, P. J.; Horn, D. M.; Hurum, D.; Jabs, W.; Larson, G.; Ly, M.; Mann, B. F.; Marx, K.; Mechref, Y.; Meyer, B.; Möginger, U.; Neusüss, C.; Nilsson, J.; Novotny, M. V.; Nyalwidhe, J. O.; Packer, N. H.; Pompach, P.; Reiz, B.; Resemann, A.; Rohrer, J. S.; Ruthenbeck, A.; Sanda, M.; Schulz, J. M.; Schweiger-Hufnagel, U.; Sihlbom, C.; Song, E.; Staples, G. O.; Suckau, D.; Tang, H.; Thaysen-Andersen, M.; Viner, R. I.; An, Y.; Valmu, L.; Wada, Y.; Watson, M.; Windwarder, M.; Whittal, R.; Wuhrer, M.; Zhu, Y.; Zou, C. (2013) “Interlaboratory Study on Differential Analysis of Protein Glycosylation by Mass Spectrometry: the ABRF Glycoprotein Research Multi-Institutional Study 2012”. Mol. Cell. Proteomics, First Published on June 13, 2013, doi:10.1074/mcp.M113.030643mcp.M113.030643.