https://doi.org/10.1351/goldbook.08318
Three-dimensional nuclear magnetic resonance spectroscopy for the assignment of protein structure with nitrogen, carbon and hydrogen dimensions.
Note:
Magnetization is transferred from \(\ce{^{1}H\upalpha}\) and \(\ce{^{1}H\upbeta}\) to \(\ce{^{13}C\upalpha}\) and \(\ce{^{13}C\upbeta}\), respectively, and then from \(\ce{^{13}C\upbeta}\) to \(\ce{^{13}C\upalpha}\). From here it is transferred first to \(\ce{^{15}NH}\) and then to \(\ce{^{1}HN}\) for detection. For each \(\ce{NH}\) group there are two \(\ce{C\upalpha}\) and \(\ce{C\upbeta}\) peaks visible. Along with the CBCA(CO)NH and HSQC this forms the standard set of experiments needed for backbone assignment.
Magnetization is transferred from \(\ce{^{1}H\upalpha}\) and \(\ce{^{1}H\upbeta}\) to \(\ce{^{13}C\upalpha}\) and \(\ce{^{13}C\upbeta}\), respectively, and then from \(\ce{^{13}C\upbeta}\) to \(\ce{^{13}C\upalpha}\). From here it is transferred first to \(\ce{^{15}NH}\) and then to \(\ce{^{1}HN}\) for detection. For each \(\ce{NH}\) group there are two \(\ce{C\upalpha}\) and \(\ce{C\upbeta}\) peaks visible. Along with the CBCA(CO)NH and HSQC this forms the standard set of experiments needed for backbone assignment.