Director, NMR Core Facility
Research Assistant Professor, Department of Biology
Rensselaer Polytechnic Institute

Education:
Ph.D. Biochemistry, University of Virginia
B.A. Chemistry, University of New Hampshire

Career Highlights:
McCallum conducted his Doctoral training under Gordon Rule at the University of Virginia and Carnegie Mellon University where he developed novel isotopic labeling strategies, NMR experiments, and computational approaches that probe structure-function relationships in large protein systems and the role of structural plasticity in the kinetics and thermodynamics of protein-ligand recognition. McCallum conducted postdoctoral training at the University of Colorado Boulder focused on developing our understanding of RNA and DNA structure and dynamics in solution and how these properties relate to function.

Prior to arriving at Rensselaer, McCallum was a Postdoctoral Research Scientist in the Department of Protein Engineering at Genentech, Inc. His research at Genentech was focused on the structural analyses of protein interactions that play key roles in the promotion or inhibition of cancer development and immune responses, and structure-based drug design of protein therapeutics.

Research Areas:
Scott McCallum is a highly experienced NMR spectroscopist and structural biologist proficient in high-resolution biomolecular NMR of complexes involving protein, RNA, DNA, carbohydrates, and drug like molecules. McCallum’s research interests are focused on defining macromolecular interactions that can be utilized in the design of drug and protein therapeutics.

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, structural basis of intein chemistry, and de novo structure determination of a putative cytokine with a key role in development.

Selected Publications:
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.