The Sumner group uses computational methods to study proteins and and bioplastics. 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 enzymes in the ubiquitin cascade. In our plastics research, we are using ab initio electronic structure methods to understand the interactions between biopolymers and plasticizers.

• Wathan, A. J.; Deschene, N. M.; Litz, J. M.; Sumner, I. “The lysine deprotonation mechanism in a ubiquitin conjugating enzyme.” The Journal of Physical Chemistry B, 2025, 128, 4962-4968. doi:10.1021/acs.jpcb.5c01486
• Iyengar, S. S.; Schlegel, H. B.; Sumner, I.; Li, J. “Rare Events Sampling Method for Quantum and Classical Ab Initio Molecular Dynamics.” The Journal of Physical Chemistry A, 2024, 128, 5386-5397. doi:10.1021/acs.jpca.3c07385
• Johnson, J. K.; Sumner, I. “On the possibility that bond strain is the mechanism of RING E3 activation in the E2-catalyzed ubiquitination reaction.” The Journal of Chemical Information and Modeling, 2022, 62, 6475-6481. (Part of the Advancing Women in Chemistry Special Issue) doi:10.1021/acs.jcim.2c00423