NMR dipole-dipole couplings between protein backbone nuclei (H-1(alpha), C-
13(alpha), N-15, H-1(N),C-13') offer enormous scope for the rapid determina
tion of protein global folds. Here, we show that measurement of one-bond sp
littings in the protein backbone is facilitated by use of protein that is s
electively isotopically enriched only in the backbone atoms. In particular,
H-1(alpha)-C-13(alpha) couplings can be measured simply and with high sens
itivity by use of conventional heteronuclear single quantum correlation (HS
QC) techniques.