The long-term goals in our research group are to understand how protein conformational ensembles are reshaped by perturbations and to quantify how these perturbations impact protein function and organismal fitness. To accomplish these goals, our group creates new computational and biophysical approaches to study how proteins move between different conformational states. A primary guiding principle of our research is that physical perturbations (such as temperature or pressure) can often reveal the same “hidden” conformations exploited by biochemical perturbations (such as ligand binding or mutation). This principle connects fundamental biophysical experiments to applied problems in protein engineering and drug design.