Sensitivity improvement in three-dimensional heteronuclear correlation NMR spectroscopy

Abstract

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