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Assignment of protein backbone resonances is most routinely carried out usingtriple resonance three dimensional NMR experiments involving amide 1H and 15Nresonances. However for intrinsically unstructured proteins, alpha-helicalproteins or proteins containing several disordered fragments, the assignmentbecomes problematic because of high degree of backbone shift degeneracy. Inthis backdrop, a novel reduced dimensionality (RD) experiment-(5,3)D-hNCO-CANH- is presented to facilitate (and/or to validate) thesequential backbone resonance assignment in such proteins. The proposed 3D NMRexperiment makes use of the modulated amide 15N chemical shifts (resulting fromthe joint sampling along both its indirect dimensions) to resolve the ambiguityinvolved in connecting the neighboring amide resonances (i.e. HiNi andHi-1Ni-1) for overlapping amide NH peaks. The experiment -encoding 5D spectralinformation- leads to a conventional 3D spectrum with significantly reducedspectral crowding and complexity. The improvisation is based on the fact thatthe linear combinations of intra-residue and inter-residue backbone chemicalshifts along both the co-evolved indirect dimensions span a wider spectralrange and produce better peak dispersion than the individual shifts themselves.Taken together, the experiment -in combination with routine triple resonance 3DNMR experiments involving backbone amide (1H and 15N) and carbon (13C-alpha and13C') chemical shifts- will serve as a powerful complementary tool to achievethe nearly complete assignment of protein backbone resonances in a timeefficient manner. The performance of the experiment and application of themethod have been demonstrated here using a 15.4 kDa size folded protein and a12 kDa size unfolded protein.

Pseudo 5D HN(C)N Experiment to Facilitate the Assignment of Backbone Resonances in Proteins Exhibiting High Backbone Shift Degeneracy