Intrinsically disordered protein regions exist in a collection of dynamic interconverting
conformations that lack a stable 3D structure. These regions are structurally heterogeneous …

The Mediator complex, which in humans is 1.4 MDa in size and includes 26 subunits,
controls many aspects of RNA polymerase II (Pol II) function. Apart from its size, a defining …

Proteins and nucleic acids can phase-separate in the cell to form concentrated biomolecular
condensates,,–. The functions of condensates span many length scales: they modulate …

Biology remains the envy of flexible soft matter fabrication because it can satisfy multiple
functional needs by organizing a small set of proteins and polysaccharides into hierarchical …

Many proteins contain large structurally disordered regions or are entirely disordered under
physiological conditions. The functions of these intrinsically disordered proteins (IDPs) often …

Our notions of protein function have long been determined by the protein structure–function
paradigm. However, the idea that protein function is dictated by a prerequisite …

Highly disordered complexes between oppositely charged intrinsically disordered proteins
present a new paradigm of biomolecular interactions. Here, we investigate the driving forces …

Nuclear magnetic resonance (NMR) has long been instrumental in the characterization of
intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). This …

Single-molecule FRET (smFRET) has become a mainstream technique for studying
biomolecular structural dynamics. The rapid and wide adoption of smFRET experiments by …

Intrinsically disordered proteins (IDPs) and multidomain proteins with flexible linkers show a
high level of structural heterogeneity and are best described by ensembles consisting of …