  The human proteome is enriched in proteins that do not fold into a stable 3D
structure. These intrinsically disordered proteins (IDPs) spontaneously
fluctuate between a large number of configurations in their native form.
Remarkably, the disorder does not lead to dysfunction as with denatured folded
proteins. In fact, unlike denatured proteins, recent evidences strongly suggest
that multiple biological functions stem from such structural plasticity. Here,
focusing on the nanoscopic length-scale, we review the latest advances in IDP
research and discuss some of the future directions in this highly promising
field.
