The nonstructural protein 1 (NS1) of the 1918 Spanish influenza A virus hijacks N-terminal
Src-homology 3 (nSH3) domain of host's cellular CrkII with exceptionally high affinity through …

Proline-rich motifs (PRMs) are widely used for mediating protein-protein interactions with
weak binding affinities. Because they are intrinsically disordered when unbound …

Many intrinsically disordered proteins (IDPs) form fuzzy complexes upon binding to their
targets. Although many IDPs are weakly bound in fuzzy complexes, some IDPs form high …

Broad conformational ensembles make intrinsically disordered proteins or regions
entropically intriguing. Although methodologically challenging and understudied, emerging …

The N-terminal repressor domain of neural restrictive silencer factor (NRSF) is an
intrinsically disordered protein (IDP) that binds to the paired amphipathic helix (PAH) …

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

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 …

Structural biology plays a pivotal role in understanding complex molecular assemblies that
encode vital functions in cellular processes. The determination of the nucleic acids, protein …

Understanding the binding behavior and conformational dynamics of intrinsically disordered
proteins (IDPs) is crucial for unraveling their regulatory roles in biological processes …

Intrinsically disordered proteins (IDPs) form biologically active complexes that can retain a
high degree of conformational disorder, escaping structural characterization by conventional …