A protein is a dynamic shape-shifter whose function is determined by the set of different structures it adopts. Unfortunately, it is impossible to directly observe most of these structures. Our lab combines computer simulations and biophysical experiments to build quantitative maps of the different shapes a protein adopts, understand the functional implications of this conformational diversity, and design new drugs and proteins. We are particularly interested in understanding and exploiting a process called allostery, which refers to communication between distant parts of a protein. Current application areas include 1) understanding and combating the evolution of antibiotic resistance, 2) inhibiting the replication of the Ebola virus, and 3) controlling signaling by G proteins and G protein-coupled receptors (GPCRs). We also develop machine learning methods and search algorithms to capture protein dynamics that are beyond the reach of a conventional simulation.

Awards and Achievements

  • NSF CAREER award