13 April 2018
Vincent Hilser
Department of Biology & T.C. Jenkins Department of Biophysics
Johns Hopkins University
Proteins are classically defined in structural terms, wherein individual sequence segments adopt specific secondary structures, which are organized hierarchically to adopt a particular native fold. We take advantage of the fact that rather than being static structures, proteins are actually ensembles of interconverting conformational states, where the native state conformations are in equilibrium with regionally or globally disordered states. This allows us to define fold specificity and stability within a unified framework, and enables characterization of fold space in energetic rather than in structural terms. My talk will focus on two areas of this emerging view of the protein ensemble. First, we will show how thermodynamic homology between structurally different folds can be used to study and design fold switching. Second, we will discuss how nature uses disorder to tune ensembles.