Coupled binding and folding of intrinsically disordered proteins: what can we learn from kinetics?

Protein or protein regions that are not forming well-defined structures in their free states under native-like conditions are called intrinsically disordered proteins. Such proteins are very common in protein-protein interactions, where their disorder apparently gives several advantages including optimal binding properties. To fully appreciate why protein disorder is advantageous for protein-protein interactions we need to understand the mechanism(s) of interaction. However, elucidating mechanisms in protein-protein interactions is usually very challenging. Here we discuss how kinetics in combination with protein engineering and structural information can be used to depict details of protein-protein interactions involving intrinsically disordered proteins.