The transcriptional coactivators CREB-binding protein (CBP) and p300 undergo a
particularly rich set of interactions with disordered and partly ordered partners, as a part of …

The last 15 years have seen a paradigm shift in our understanding of protein biochemistry,
with the realization that an unexpectedly high fraction of the human genome codes for …

The functions of intrinsically disordered proteins (IDPs) are governed by relationships
between information encoded in their amino acid sequences and the ensembles of …

Intrinsically disordered proteins (IDPs) frequently function in protein interaction networks that
regulate crucial cellular signaling pathways. Many IDPs undergo transitions from disordered …

Intrinsically disordered proteins (IDPs) play important roles in cellular functions. The inherent
structural heterogeneity of IDPs makes the high-resolution experimental characterization of …

Despite playing important roles throughout biology, molecular recognition mechanisms in
intrinsically disordered proteins remain poorly understood. We present a combination of …

Intrinsically disordered proteins participate in important protein–protein and protein–nucleic
acid interactions and control cellular phenotypes through their prominence as dynamic …

The dynamic modes and time scales sampled by intrinsically disordered proteins (IDPs)
define their function. Nuclear magnetic resonance (NMR) spin relaxation is probably the …

Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing
essential roles in all aspects of cellular and extracellular biochemistry. To understand their …

Intrinsically disordered proteins play an important role in cellular signalling, mediated by
their interactions with other biomolecules. A key question concerns the nature of their …