N TAIL provides an interesting model system for the study of the interaction of an intrinsically disordered protein and its partners. Its multiple-site mode of interaction well illustrates the complexity of the contacts established by intrinsically disordered proteins and emphasizes the need for thorough investigations of the molecular mechanisms underlying recognition of the partner. Indeed, binding of disordered regions to their targets involves different types of interactions, such as binding coupled to folding, binding with no gain of regular secondary structure, or coexistence of both interaction mechanisms (for a review, see Dyson and Wright 2005) .