Despite the partial disorder‐to‐order transition that intrinsically disordered proteins often
undergo upon binding to their partners, a considerable amount of residual disorder may be …

Disordered proteins often act as interaction hubs in cellular pathways, via the specific
recognition of a distinguished set of partners. While disordered regions can adopt a well …

Numerous relatively short regions within intrinsically disordered proteins (IDPs) serve as
molecular recognition elements (MoREs). They fold into ordered structures upon binding to …

Intrinsically disordered proteins (IDPs) interact with globular proteins through a variety of
mechanisms, resulting in the structurally heterogeneous ensembles known as fuzzy …

Disordered proteins frequently serve as interaction hubs involving a constrained variety of
partners. Complexes with different partners frequently exhibit distinct binding modes …

Protein interactions involving intrinsically disordered proteins (IDPs) greatly extend the
range of binding mechanisms available to proteins. In interactions employing coupled …

In this paper we review our recent findings on the different interaction mechanisms of the C-
terminal domain of the nucleoprotein (N) of measles virus (MeV) NTAIL, a model viral …

Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific
localized contacts and target-induced disorder to order transitions. However, some IDPs …

In view of getting insights into the molecular determinants of the binding efficiency of
intrinsically disordered proteins (IDPs), we used random mutagenesis. As a proof of concept …

Intrinsically disordered proteins (IDPs) are functionally active despite lacking a well-defined
three-dimensional structure. Such proteins often undergo a disorder-to-order transition, or …