Chemistry Faculty:
Robert J. Woods, Ph.D.
Associate Professor
Phone: 706-542-4454
E-mail: rwoods@ccrc.uga.edu
Biographical Information
Ph.D., Queen's University of Kingston, Ontario, 1990
Associate Member, University of Oxford, UK, 1991-93
Research Interests
Research in the Woods group examines the relationship between carbohydrate conformation and biological recognition. Areas of particular interest include carbohydrate antigenicity in immunological events, carbohydrate-processing enzymes, and the development of appropriate simulational methods for these systems. The flexibility of biomolecules is ideally suited to analysis by molecular dynamics simulations, whereas quantum mechanical methods are applied to examine enzyme mechanisms and develop force field parameters. The relationship between carbohydrate sequence/structure and the affinity of carbohydrate-protein interactions is amenable to study by free energy perturbation and direct deltaG calculations. The computational methods are complimented by experimental techniques, such as NMR spectroscopy, X-ray crystallography, and mass spectrometry.
The computational simulations use the all-atom AMBER force field for proteins and a novel set of force field parameters ( GLYCAM) developed by the Woods group for use with carbohydrates. The GLYCAM parameters make it possible to simulate the interatomic interactions responsible for oligosaccharide and glycoprotein dynamics and compare these directly with experimental NMR data that are often consistent with numerous possible conformations. These parameters are currently suitable for all biologically relevant N- and O-linkages in oligo- and polysaccharides and glycoproteins.
Further aspects of the research include structural studies of peptides that are able to inhibit carbohydrate-protein interactions. Such peptides can be said to mimic the carbohydrates, particularly so when the peptides are also able to induce an anti-carbohydrate immune response. These studies involve crystallographic analysis of peptide-protein complexes, in which the peptide is bound to a carbohydrate binding protein. Peptides that can inhibit carbohydrate interactions are possible lead candidates for drugs to combat inflammation and diseases that depend on carbohydrate recognition. Further, these peptides are potentially useful as anti-bacterial vaccines. These aspects are being examined in collaboration with research groups here at UGA and at the Research Institute for Children in New Orleans.
| - See Also: - |
| - Link to research group website - |
Publications
J.-R. Brisson, S. Uhrinova, R.J. Woods, M. van der Zwan, H.C. Jarrell, L.C. Paoletti, D.L. Kasper, H.J. Jennings, Biochemistry 1997, 36, 3278-3292.
R.J. Woods, R.A. Dwek, C.J. Edge, B. Fraser-Reid, J. Phys. Chem. 1995, 99, 3832-3846.
R.J. Woods, Curr. Opin. Struct. Biol. 1995, 5, 591-598.