Professor 1990: Ph.D. (Computational and Carbohydrate Chemistry), School of Graduate Studies and Research, Queen's University 1985: B.Sc. (Honors, Engineering Chemistry), Faculty of Applied Science, Queen's University at Kingston, Ontario, Canada Office: 1089 CCRC Contact Phone Number: 542-4454 Lab: 2069 CCRC Lab Phone: 542-3508 Fax Number: 542-4412 E-mail: rwoods@ccrc.uga.edu Additional Information / Lab Page

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 the GLYCAM 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 ΔG calculations.

The computational methods are complemented by experimental techniques, such as NMR spectroscopy, X-ray crystallography, and mass spectrometry.

Selected Recent Publications

• Tschampel, S. M., Kennerty, M. R., and Woods, R.J.  2007. A TIP5P-Consistent Treatment of Electrostatics for Biomolecular Simulations. J. Chem. Theory Comput., In Press.
  
  
• Elking, D., T. Darden and R.J. Woods. 2006. Gaussian Induced Dipole Polarization Model. J. Comput. Chem. 28, 1261-1274.
  
  
• Seyfried, N. T., J. A. Atwood, III, A. Almond, A. J. Day, R. Orlando, R. J. Woods. 2007. Fourier transform mass spectrometry to monitor hyaluronan–protein interactions: use of hydrogen/deuterium amide exchange, Rapid Commun. Mass Spectrom. 21, 121-131.
  
  
• Kadirvelraj, R., M.L. Beckham, M. G. Ford Gonzalez Outeriño, J. and R.J. Woods.  2006. Understanding the bacterial polysaccharide antigenicity of Streptococcus agalactiae versus Streptococcus pneumoniae.  Proc. Natl. Acad. Sci. USA. 103, 8149-8154.
  
  
• Kawatkar, S.P., Kuntz, D.A., Woods, R.J., Rose, D.R., Boons, G.J. 2006. Structural Basis of the Inhibition of Golgi α-Mannosidase II by Mannostatin A and the Role of the Thiomethyl Moiety in Ligand-Protein Interactions. J. Am. Chem. Soc. 128, 8310-8319.
  
  
• Gonzalez-Outeiriño, J., K.N. Kirschner, S. Thobhani, and R.J. Woods. 2006. Reconciling solvent effects on rotamer populations in carbohydrates: a joint MD and NMR analysis. Can. J. Chem. 84, 569-579.
  
  
• Case, D.A., T. Cheatham, T. Darden, H. Gohlke, R. Luo, K.H. Merz, Jr., A. Onufriev, C. Simmerling, B. Wang, R.J. Woods. 2005. The AMBER biomolecular simulation programs. J. Comput. Chem. 26, 1668-1688.
  
  
• Gonzalez Outeriño, J., R. Kadirvelraj and R. J. Woods. 2005. Structural elucidation of type III group B Streptococcus capsular polysaccharide using molecular dynamics simulations: the role of sialic acid. Carbohydr. Res. 340, 1007-1018.
  
  
• Li, B., S. Kawatkar, S. George, H. Strachan, R.J. Woods, A. Siriwardena, K.W. Moremen, G.-J. Boons. 2005. Inhibition of Golgi Mannosidase II with Mannostatin A Analogues: Synthesis, Biological Evaluation, and Structure-Activity Relationship Studies. Chembiochem 5: 1220-1227.