The Importance of Intrinsic Order in a Disordered Protein Ligand

Over the last decade, it has become increasingly apparent that a significant number of proteins do not form stable tertiary structures, but instead dynamically sample a broad range of largely disordered states (1). Generally referred to as intrinsically disordered proteins (IDPs), these species can be associated with a range of functions, and often serve as hub proteins that bind to multiple targets (2). Binding events involving IDPs are commonly accompanied by the formation of defined structure. [PUBLICATION ABSTRACT]