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Since the information on molecular conformations in NMR experiments is retrieved from the analysis of the unique chemical shift signals generated by the local environment of each atomic nucleus, and since no stable local environment for chemical groups is present in IDPs/IDRs, NMR spectra of IDPs are different from those of ordered proteins and contain some peculiar characteristics, such as the limited dispersion in proton NMR ( c ) under various conditions, Arthur Kowalsky reported that although the peaks in the proton NMR spectra of native proteins are broad, they became sharper under various denaturing conditions (Kowalsky, 1962)