Flavonoid glycosides represent a large class of compounds that are ubiquitous and often relatively abundant in vascular plants. For biosynthetic reasons, flavonoids typically occur as conjugates with sugar moieties, which often amount to three or more sugars, thereby reaching the molar mass range ~800 g/mol to 1,100 g/mol. The close stereochemical relationships between the sugar moieties and the variable inter-glycosidic linkages explain the challenges associated with the structure elucidation of such compounds. For example, specific triglycosides of quercetin and kaempferol are important plant-organ specific quality markers of the medicinal plant, Ashwagandha (Withania somnifera). As the compounds contain robinose (α-L-Rha11→ 6 β-D-Gal) or rutinose (α-L-Rha11→ 6 β-D-Glc) and β-D-glucose, they give rise to many near-degenerate resonances, which can be fully understood by HiFSA . While otherwise concealed by multiplet designation, the NMR spectra of these flavonoid glycosides contain highly structure-specific peak patterns with a myriad of underlying lines, all of which can be fully assigned to the individual H atoms. Importantly, the HiFSA-based understanding of the spectra allows the distinction and identification of close congeners, and even enables their analysis by benchtop NMR . Also representing oligomers of congeneric building blocks, peptides are another class of higher molecular weight compounds that challenge HNMR spectroscopic data interpretation. For example, a recent systematic study of the spin systems of linear oligopeptides up to the size of the octapeptide, angiotensin II (1,046 amu) and the nonapeptide, oxytocin (1,067 amu), demonstrated the feasibility of HNMR spectroscopy to perform an NMR-based structural sequencing (HiFSA sequencing) of the peptides . Approaching oxytocin via stepwise synthesis, the study showed how each individual amino acid and substituent chemical shift (s.c.s.) effects contribute to the final spectrum. The outcomes also revealed that the characteristics of the resonances of the individual amino acid moieties show certain variation in terms of observed patterns, but almost no variation of the underlying spin couplings. This highlights the relevance of full spin system analysis in the understanding of HNMR spectra as well as the importance of distinguishing between patterns, peaks, and lines when performing visual and numerical interpretation.