The Sumner group uses and develops computational methods to study proteins and to probe fundamental chemical concepts like bonding. In our protein research, we aim to understand the structural properties of proteins as well as the catalytic mechanisms of enzymes. To accomplish these goals, we utilize molecular dynamics, a technique that generates molecular trajectories based on classical (Newton’s) equations of motion, and quantum chemical methods, a technique that can calculate bond breaking/formation energies. We are currently studying the catalytic mechanisms of ubiquitin and histone acetyl transferases. We are also developing a new quantum mechanical technique to study chemical properties like bonding and partial atomic charges. This technique is based on quantum hydrodynamics and involves computing electron trajectories.

• W. M . Jones, A. G. Davis, R. H. Wilson, K. L. Elliott, and I. Sumner "A Conserved Asparagine in a Ubiquitin Conjugating Enzyme Positions the Substrate for Nucleophilic Attack" J. Comput. Chem., 40. (2019), 1969-1977. DOI:10.1002/jcc.25852
• H. Bunn, R. M. Soliday, I. Sumner and P. L. Raston “Far-infrared spectroscopic characterization of anti-vinyl alcohol” The Astrophysical Journal, 847. (2017), 67-72. DOI: 10.3847/1538-4357/aa8870
• R. H. Wilson, S. Zamfir, and I. Sumner “Molecular dynamics simulations reveal a new role for a conserved active site asparagine in a ubiquitin-conjugating enzyme” J. Mol. Graph. Model. 76 (2017), 403-411. DOI: 10.1016/j.jmgm.2017.07.006