The common notion in the protein world holds that proteins are synthesized as a linear polypeptide chain, followed by folding into a unique, functional 3D-structure. As outlined in many articles of this volume, this is in fact the case for a great proportion of the proteome. Many proteins and protein domains, however, are intrinsically disordered (IDPs), i.e., they cannot fold on their own, but often undergo a folding transition in the presence of a binding partner. This binding-induced folding process shows strong conceptual parallels with the folding of globular proteins, in a sense that it can proceed via two routes, either induction of the folded conformation from an initial random state or selection of a pre-formed state already present in the ensemble. In addition, we show that IDPs not only undergo folding themselves, they also assist the folding process of other proteins as chaperones, and even contribute to the quality control processes of the cell, in which irreparably misfolded proteins are recognized and tagged for proteasomal degradation. These various mechanisms suggest that structural disorder, in a biological context, is linked with protein folding in several ways, in which both the IDP and its partner may undergo reciprocal structural transitions.