Membrane proteins act like a molecular switchboard, integrating extracellular chemical and mechanical stimuli to produce specific intracellular responses to environmental changes. These switch-like responses require that membrane proteins undergo conformational rearrangements, or changes in their three-dimensional shape.

In our lab, we capture the atomic-level details of these rearrangements with experimental biophysics and biomolecular simulation. We seek to understand how variation in protein sequence and changes to the local chemical environment modulate these dynamics. Our research aims to exploit this information to discover new ligands that tune membrane protein function to improve therapeutic benefits while avoiding undesirable side effects.