Research Assistant Professor
Director, NMR Core Facility
Education and Training
Ph.D. University of Virginia
Office Tel: (518) 276-2856
Lab Tel: (518) 276-4286
Office: Center for Biotechnology and Interdisciplinary Studies Rm. 1143
Rensselaer Polytechnic Institute
110 8th Street
Troy, NY 12180
My research interests are focused on identifying macromolecular interactions that have key roles in major diseases including cancer and that can be utilized in the design of drug and protein therapeutics. Research projects are highly diverse and primarily utilize high-resolution biomolecular NMR to investigate the structural basis for binding specificity in the formation of complexes involving protein, RNA, DNA, carbohydrates, and drug like molecules.
Current projects include elucidating the structure-function relationships of heparin in the formation of protein complexes central to cancer, investigating structure-activity relationships among anthrax inhibiting peptides and their receptors, defining the structural basis of intein chemistry and evaluating this enzyme as a novel target for tuberculosis therapeutics, and de novo structure determination of a putative cytokine with a key role in development.
Sgourakis, N.G., Yan, Y., McCallum, S.A., Wang, C, and Garcia, A. E. Probing the solution structure of the Alzheimer’s peptides. (In Press, Journal of Molecular Biology)
Wiesman,C., Katschke, K.J., Yin, J., Helmy, K.Y., Steffek, M., Fairbrother, W.J., McCallum, S.A., Embuscado, L., DeForge, L., Hass, P., and van Lookeren Campagne, M. (2006) Structure of complement receptor CRIg bound to C3b provides insight into the regulation of complement activation. Nature 444, 217-220
McCallum, S.A., Bazan, J.F., Merchant, M., Yin, J.P., Pan, B., de Sauvage, F.J., and Fairbrother, W.J. (2006) Structure of SAP18: A ubiquitin fold in histone deacetylase complex assembly. Biochemistry 45, 11974-11982.
Latham, M.P., Brown, D.J., McCallum, S.A. and Pardi A. (2005) NMR methods for studying the structure and dynamics of RNA. CHEMBIOCHEM 6, 1492-1505.
Vermeulen, A, McCallum, S.A. and Pardi, A. (2005) Comparison of global structure and dynamics of native and unmodified tRNAval. Biochemistry 44, 6024-6033.
McCallum, S.A. and Fairbrother, W.J. (2005) 1H, 13C, and 15N resonance assignments of SAP18, a substrate adapter molecule for the SIN3A histone deacetylase complex. Journal of Biomolecular NMR 31, 259.
Juker, F.M., McCallum, S.A., Phillips, R. and Pardi, A. (2003) Role of a heterogeneous free state in the formation of a specific RNA-theophylline complex. Biochemistry 42, 2560-2567.
McCallum, S.A. and Pardi, A. (2003) Refined solution structure of the iron responsive element RNA using residual dipolar couplings. Journal of Molecular Biology 326, 1037-1050.
Hitchens, T.K., McCallum, S.A., and Rule, G.S. (2003) On reliable chemical shift assignments in deuterated proteins. Journal of Biomolecular NMR 25, 11-23.
Hitchens, T.K., Lukin, J.A., Zhan, Y., McCallum, S.A., and Rule, G.S. (2003) MONTE: An automated Monte Carlo based approach to nuclear magnetic resonance assignment of proteins. Journal of Biomolecular NMR 25, 1-9.
McCallum, S.A., Hitchens TK, Torborg C, and Rule, G.S. (2000) Ligand-induced changes in the structure and dynamics of a human class Mu glutathione S-transferase. Biochemistry 39,7343-7356.
Hitchens, T.K., McCallum, S.A., Rule, G.S. (1999). A J(CH)-modulated 2D (HACACO)NH pulse scheme for quantitative measurement of 13Ca-1Ha couplings in 15N, 13C-labeled proteins. Journal of Magnetic Resonance 140, 281-284.
McCallum, S.A., Hitchens, T.K. and Rule, G.S. (1998). Solution structure of the carboxy-terminus of a human class mu glutathione S-transferase: NMR assignment strategies in large proteins. Journal of Molecular Biology 285, 2119-2132.
McCallum, S.A., Hitchens, T.K., and Rule, G.S. (1998) Unambiguous correlations of backbone amide and aliphatic gamma resonances in deuterated proteins. Journal of Magnetic Resonance 134, 350-354.