ArticleMethods in molecular biology (Clifton, N.J.)2025
Chemical Shift Analysis of Oligosaccharides.
Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
More than 50% of all eukaryotic proteins are glycosylated. Protein glycosylation, the addition of sugar molecules to the protein backbone, significantly impacts their structure, function, and interactions, thereby playing pivotal roles in numerous biological processes. Nuclear magnetic resonance (NMR) spectroscopy is a powerful tool for deciphering the complexity of glycoprotein structures and is particularly well-suited for the detailed analysis of their glycan composition. This chapter provides a description of the NMR procedures specifically tailored for the chemical shift assignment of glycoprotein oligosaccharides. Details regarding isotope-labeling strategies, advanced pulse sequences, and data analysis are discussed, highlighting the potential of NMR techniques to enhance our understanding of glycoprotein functions.
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