Conformational Entropy of Disordered Polypeptides and its Elusive Contribution to the Thermodynamics of Protein Binding

Justin Drake, Ohio Supercomputer Center

Usage Details

For most of the 20th century it was widely believed that the relatively well-defined structure of a protein dictated its function. However, over the past decade it has become clear that many proteins rely on intrinsically disordered regions (IDRs) to bind other proteins and carry out their function. IDRs may fold, unfold, or redistribute their conformational ensemble upon binding to their targets. The thermodynamic coupling of these events with the free energy of protein binding remains obscure. In this project, Justin Drake will use molecular simulations and computational biophysics to examine the extent of which conformational entropy of IDRs contributes, or even dominates, the free energy of protein binding.