Editing of multiplicity in two- and three-dimensional heteronuclear NMR spectroscopy by Fourier transformation of the pulse-angle dependency
P. Schmieder, T. Domke, D.G. Norris, M. Kurz, H. Kessler, D. Leibfritz
J. Magn. Reson. (1991) 93, 430-435
In order to make use of the high sensitivity of an inverse editing sequence in addition to the editing capabilities of a flip-angle variation, the DEPT-HMQC (distortionless enhancement by polarization transfer-heteronuclear multiple quantum coherence) pulse sequences are combined with the incrementation of the pulse angle. llustrative results obtained by applying both 2- and 3-dimensional procedures to a cyclic hexapeptide are shown. The method of introduction of a further dimension in heteronuclear NMR spectroscopy by variation of the pulse angle is generally applicable and results in an increased dispersion according to multiplicity. For spectra of peptides and/or proteins, these spectra provide a suitable differentiation of several amino acids in different spectral planes.