Conformational characterization of a protein complex involving intrinsically disordered protein by small-angle neutron scattering using the inverse contrast matching method: a case study of interaction between α-synuclein and PbaB tetramer as a model chaperone

Finely tuned protein deuteration enabled selective observation of small-angle neutron scattering of an intrinsically disordered protein (IDP) captured by a tetrameric molecular chaperone. The data thus obtained provided unique information on the conformational changes of the IDP coupled with interaction with the chaperone, and complemented the NMR approach.