Editing of multidimensional NMR spectra of partially deuterated proteins. Measurement of amide deuterium isotope effects on the chemical shifts of protein backbone nuclei.

Novel multidimensional NMR pulse sequences are presented for determination of amide deuterium isotope effects on the 13C chemical shifts of the backbone in proteins. The sequences edit heteronuclear triple resonance spectra into two subspectra according to whether a deuterium or a proton is attached to 15N for the pertinent correlations. The new experiments are demonstrated using 13C, 15N-labeled RAP 17-112 (N-terminal domain of α2-macroglobulin receptor associated protein).