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Sequence specific resonance assignment and secondary structure determinationof proteins form the basis for variety of structural and functional proteomicsstudies by NMR. In this context, an efficient standalone method for rapidassignment of backbone (1H, 15N, 13Ca and 13C') resonances and secondarystructure determination of proteins has been presented here. Compared tocurrently available strategies used for the purpose, the method employs only asingle reduced dimensionality (RD) experiment -(4,3)D-hnCOCANH and exploits thelinear combinations of backbone (13Ca and 13C') chemical shifts to achieve adispersion relatively better compared to those of individual chemical shifts(see the text) for efficient and rapid data analysis. Further, the experimentleads to the spectrum with direct distinction of self (intra-residue) andsequential (inter-residue) carbon correlation peaks; these appear opposite insigns and therefore can easily be discriminated without using an additionalcomplementary experiment. On top of all this, the main strength of the methodis its efficient and robust assignment strategy based on: (a) multiple, butunidirectional sequential 15N and 13C correlations (i-->i-1) and (b) thedistinctive peak patterns of self and sequential peaks in different[(F1(13C)-F3(1H) and (F2(15N)-F3(1H)] planes of the 3D spectrum which enableready identification of certain specific triplet sequences (see the text) andthus serve as check points for mapping the stretches of sequentially connectedHSQC cross peaks on to the primary sequence for assigning the resonancessequence specifically. Overall, the standalone method presented here will be animportant backbone assignment tool for structural and functional proteomics,protein folding, and drug discovery research programs by NMR.

Reduced Dimensionality (4,3)D-hnCOCANH Experiment: An Efficient Backbone Assignment tool for NMR studies of Proteins