https://doi.org/10.1351/goldbook.08363
Three-dimensional nuclear magnetic resonance spectroscopy for the assignment of protein structure with nitrogen, carbon and hydrogen dimensions.
Note:
The magnetization is passed from \(\ce{^{1}H}\) to \(\ce{^{15}N}\) and then via the \(\ce{N-C\upalpha}\) \(\rm{J}\mbox{-}\rm{coupling}\) to the \(\ce{^{13}C\upalpha}\) and then back again to \(\ce{^{15}N}\) and \(\ce{^{1}H}\) hydrogen for detection. Each \(\ce{NH}\) group will show correlations to both their own and the previous residue’s \(\ce{^{13}C\upalpha}\).
The magnetization is passed from \(\ce{^{1}H}\) to \(\ce{^{15}N}\) and then via the \(\ce{N-C\upalpha}\) \(\rm{J}\mbox{-}\rm{coupling}\) to the \(\ce{^{13}C\upalpha}\) and then back again to \(\ce{^{15}N}\) and \(\ce{^{1}H}\) hydrogen for detection. Each \(\ce{NH}\) group will show correlations to both their own and the previous residue’s \(\ce{^{13}C\upalpha}\).