Using umbrella-sampling methods to sample rare configurations, we uncover reaction landscapes of how proteins facilitate chemistry to uncover novel insight into mechanisms.
Every atom in a protein is subject to forces that allow them to move. Leveraging path-sampling algorithms, we explore how proteins employ dynamics in order to cross reaction barriers, and how this gives rise to reactivity.
Structural features of a protein can be highly predictive of successful reactions. In the following work, we explore how geometry of the active-site relates to quantitated electronic mechanism in an enzyme.