Intrinsically disordered regions (IDRs) are especially enriched among proteins that regulate
chromatin and transcription. As a result, mechanisms that influence specificity of IDR-driven …

Intrinsically disordered regions (IDRs) make up ca. 30% of the proteome of most eukaryotes,
and are involved in a diverse set of functions. Conventional sequence alignment tools …

The traditional structure to function paradigm conceives of a protein's function as emerging
from its structure. In recent years, it has been established that unstructured, intrinsically …

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

Intrinsically disordered protein regions (IDRs) pervasively engage in essential molecular
functions, yet they are often poorly conserved as assessed by sequence alignment. To …

Eukaryotic transcription factors (TFs) are the final integrators of a complex molecular
feedback mechanism that interfaces with the genome, consolidating information for …

In recent years, it has become quite evident that numerous proteins exist as an ensemble of
conformers that collectively appears to be intrinsically disordered (ID). Of particular …

Intrinsically disordered proteins (IDPs) are important components of the cellular signalling
machinery, allowing the same polypeptide to undertake different interactions with different …

Increased understanding of intrinsically disordered proteins (IDPs) and protein regions has
revolutionized our view of the relationship between protein structure and function. Data now …

Highlights•Protein disorder is highly over-represented within transcriptional
processes.•Protein disorder may accelerate binding, unbinding and/or DNA search …