Syracuse

We report enhanced sensitivity NMR measurements of intrinsically disordered proteins (IDPs) in the presence of paramagnetic relaxation enhancement (PRE) agents such as Ni 2+ -chelated DO2A. In proton-detected 1 H-15 N SOFAST-HMQC and carbon-detected (H-flip) 13 CO-15 N experiments, faster longitudinal relaxation enables the usage of even shorter interscan delays. This results in higher NMR signal intensities per units of experimental time, without adverse line broadening effects. At 40 mmol.L -1 of the PRE agent, we obtain a 1.7to 1.9-fold larger signal to noise (S/N) for the respective 2D NMR experiments. High solvent accessibility of IDP residues renders this class of proteins particularly amenable to the outlined approach.