Die dynamische Funktion intrinsisch ungeordneter Proteine

In contrast to folded proteins, intrinsically disordered proteins (IDPs) exert their functions in the absence of a stable three-dimensional structure. They are active in many important cellular mechanisms, for example cell signaling and transcriptional regulation and thus very important cellular players. Their dynamics make them extremely difficult to study, but recent advances in solution based structural biology techniques have increased the understanding of IDPs’ functions on a molecular level.