New multidimensional editing experiments for measurement of amide deuterium isotope effects on C-beta chemical shifts in C-13, N-15-labeled proteins

Novel multidimensional NMR pulse sequences for measurement of the three- an d four-bond amide deuterium isotope effect on the chemical shifts of C-13(b eta) in proteins are presented. The sequences result in editing into two su bspectra of a heteronuclear triple resonance spectrum {omega(N), omega(C be ta), omega(H-alpha)} according to there being a deuterium or a proton attac hed to N-15 for the pertinent correlations. The new experiments are demonst rated by an application to the first module of the C-13, N-15-labeled prote in RAP 18-112 (N-terminal module of alpha(2)-macroglobulin receptor associa ted-protein). (C) 1998 Academic Press.