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

Phosphorylation is the most common post-translational modification (PTM) in eukaryotes,
occurring particularly frequently in intrinsically disordered proteins (IDPs). These proteins …

Many intrinsically disordered proteins (IDPs) may undergo liquid–liquid phase separation
(LLPS) and participate in the formation of membraneless organelles in the cell, thereby …

Molecular dynamics (MD) simulation is a valuable tool for characterizing the structural
dynamics of folded proteins and should be similarly applicable to disordered proteins and …

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

All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which
makes their structural characterization challenging. Although challenging, characterization …

The assembly of individual proteins into functional complexes is fundamental to nearly all
biological processes. In recent decades, many thousands of homomeric and heteromeric …

The suggestion that the native state of many proteins is intrinsically disordered (or, as
originally termed, unstructured) is now integral to our general view of protein structure and …