Nuclear Magnetic Resonance (NMR) spectroscopy is an important technique used for structural and dynamical characterizations of a wide variety of molecules ranging from small organic molecules to large protein complexes. These characterizations include biomolecular structure and dynamics studies, as well as conformational and configurational analysis of small molecules such as natural products and synthetic drug-like molecules. For small molecules, proton ( 1 H) NMR spectroscopy has been proven to provide critical insight because of the high sensitivity offered by the large inherent gyromagnetic ratio and natural abundance of 1 H. However, H NMR spectral resolution suffers significantly from the presence of severely overlapped homonuclear scalar coupling multiplets. These complex multiplet patterns can in favorable cases be resolved to create resolved singlet peaks at the respective chemical shifts (pure shifts) using homonuclear decoupling NMR methods. This improvement in the spectral resolution can be up to an order of magnitude, however, at a trade-off of spectral sensitivity of up to two orders of magnitude per unit of experimental measurement time, if a homonuclear broadband decoupling scheme is considered. Although homonuclear bandselective decoupling can offer full sensitivity, it only applies to a single group of signals and it is not applicable if any scalarly coupled spins coexist in the chosen frequency range. For complex NMR spin systems, such as those present in steroids and saccharides, it is, therefore, necessary to consider broadband pure shift NMR methods to obtain the required highresolution pure chemical shift spectrum. Conversely, because of the low sensitivity of these methods, it is not possible to detect insensitive signals while using these broadband decoupling schemes. This, in turn, calls for new strategies to improve the spectral sensitivity of pure shift NMR experiments.