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Updated: Sep 13, 2025

Mass Spectrometric Analysis of Glycosphingolipid Antigens
Published on: April 16, 2013
Chemical Shift Analysis of Oligosaccharides
Ana Ardá1,2, Ana Gimeno3,4, Luca Unione3,4
1Chemical Glycobiology Lab, Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Derio, Bizkaia, Spain. aarda@cicbiogune.es.
None:
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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