Protein Unfolding by Using Residual Dipolar Couplings

Natively unfolded regions have been shown to be common in functional proteins in a vast range of biochemical processes. In contrast to classical structural biology, unfolded proteins must be described by an ensemble of intermediate conformers. The traditional NMR approach, which has been widely used for structure determination in classical structural biology, is still feasible for the study of unstructured proteins in solution, since the NMR experimental data, such as chemical shifts, residual dipolar couplings (RDCs), etc., can be still measured in highly disordered states, and thus used for the characterization of average properties over the ensemble of conformers.