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Although two-dimensional proton homonuclear NMR techniques have proven successful for molecules of size up to - IO4 Da (I), larger and more complex systems are not amenable to complete study by these methods due to excessive overlap of resonances. In such cases, the larger chemical-shift dispersion of “N or r3C nuclei can be used to alleviate overlap problems (2-4). Three-dimensional heteronuclear NMR
spectroscopy of isotopically enriched proteins (5,6) has been shown to be an efficient method of overcoming resonance congestion in complex protein spectra ( 7-9). Recent reports (10-12) indicate the feasibility of heteronuclear 3D NMR spectroscopy for structural investigations of polysaccharides and glycoproteins as well.
In this Communication, methods are presented that provide up to a \lj: improvement
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