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Updated: Aug 30, 2026

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
Published on: May 17, 2024
New structural insights into carbohydrate-protein interactions from NMR spectroscopy
Heide Kogelberg1, Dolores Solís, Jesús Jiménez-Barbero
1The Glycosciences Laboratory, Faculty of Medicine, Imperial College London, Northwick Park Institute of Medical Research, Harrow, Middlesex, HA1 3UJ, UK. h.kogelberg@imperial.ac.uk
Abstract:
Recently developed NMR methods have been applied to discover carbohydrate ligands for proteins and to identify their binding epitopes. The structural details of carbohydrate-protein complexes have also been examined by NMR, providing site-specific information on the architecture, binding selectivity and plasticity of the carbohydrate-binding sites of the proteins. New insights into the conformational behaviour of free and protein-bound glycomimetics pave the way for the design of carbohydrate-based therapeutics. Finally, recent progress towards elucidating the influence of glycosylation on peptide conformation will be of key importance to fully understanding the role of carbohydrates in the function of glycopeptides.
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