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

Highlights•IDRs exist as diverse and dynamic populations of interchanging structural
conformations.•Subsets of these conformations can have distinct functions.•Cell state …

Intrinsically disordered proteins (IDPs) carry out many biological functions. They lack a
stable three-dimensional structure, but rather adopt many different conformations in dynamic …

The interactions of intrinsically disordered proteins (IDPs) with their molecular targets are
essential for the regulation of many cellular processes. IDPs can perform their functions …

It is becoming increasingly clear that eukaryotic cell physiology is largely controlled by
protein–protein interactions involving disordered protein regions, which usually interact with …

Disordered proteins frequently serve as interaction hubs involving a constrained variety of
partners. Complexes with different partners frequently exhibit distinct binding modes …

Disordered proteins often act as interaction hubs in cellular pathways, via the specific
recognition of a distinguished set of partners. While disordered regions can adopt a well …

Highlights•Suboptimal binding motifs lead to frustrated energy landscape.•Non-native,
transient contacts regulate heterogeneity in transition or bound state.•Alternative recognition …

Highlights•Mutational effects are consistently felt beyond the first shell of
interactions.•Mutations modulate the dynamics and chemical shifts of distal …

Polyubiquitin chains are flexible multidomain proteins, whose conformational dynamics
enable them to regulate multiple biological pathways. Their dynamic is determined by the …