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

… The term "intrinsic disorder" allows for the ability of the chain to conditionally fold in some …
the presence of binding partners. We note that IDPs are fully disordered proteins with no folded …

… IDPs adopt a heterogeneous structural ensemble, in contrast … of the role of intrinsic disorder
in biological mechanisms has … new approaches to interrogate protein structure and function, …

… completely disordered, either as an intrinsically disordered protein (IDP) or having specific …
structural heterogeneity, as seen in IDPs/IDRs, and their role in biological recognition, binding …

… , and protein binding (eg, Wiskott–Aldrich syndrome protein (… reduce the overall conformation
heterogeneity of the IDRs as … to explain the molecular mechanisms of the pathogenesis of …

… including their conformational heterogeneity, protein–protein interactions, and the phase
transition of biomolecular condensates that are central to various biological functions. Besides, …

… protein structure and function relationship emerged with the discovery of intrinsically disordered
proteins (IDPs) and intrinsically … and flexibility, resulting in conformational heterogeneity. …

… structure. They also initiated massive efforts on the analyses of molecular mechanisms of
protein … 200 K) to investigate the structural heterogeneity of two copper proteins, azurin and …

… examined comprise intrinsically disordered proteins (IDPs) (or regions within ordered proteins,
referred to as intrinsically disordered regions or IDRs) that lack rigid structure in the native …

… entails proteins binding to their partners and the intrinsic … level of their structural heterogeneity
in the bound state and exert … To gain insight into the molecular mechanisms involved with …