Folding of Disordered Proteins: Single Molecules to Mesoscales

Abstract

Intrinsic protein disorder is increasingly being recognized as prevalent in proteomes and important in a number of cellular functions. Many intrinsically disordered proteins (IDPs) display coupled folding and binding to partners, a functionally important aspect of their biophysics that is often difficult to study using standard ensemble methods. By avoiding the averaging out of information over an ensemble, single-molecule experiments can shed mechanistic light on such binding-folding reactions, with layers of complexity emerging due to multicomponent interactions. Overall, the results will highlight the strengths of single-molecule methods to reveal functionally important complexity at the molecular and mesoscale levels in IDP binding-folding landscapes.