Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins

Intrinsically disordered proteins (IDPs) are highly flexible and undergo disorder to order transition upon binding. They are highly abundant in human proteomes and play critical roles in cell signaling and regulatory processes. This review mainly focuses on the dynamics of disordered proteins including their conformational heterogeneity, protein–protein interactions, and the phase transition of biomolecular condensates that are central to...