Related Experiment Video
Updated: Feb 26, 2026

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
Published on: August 26, 2025
Simple Gd3+-Neu5NAc complexation results in NMR chemical shift asymmetries of structurally equivalent complex-type
Konstantin Usachev1, Yoshiki Yamaguchi, Masayuki Takamatsu
1NMR Laboratory, Institute of Physics, Kazan Federal University, 18 Kremlyovskaya street, Kazan 420008, Russia.
Abstract:
In the present Communication, we propose a quite simple but previously overlooked approach for conveniently analyzing, assigning, and extracting sialic acid-containing N-glycan structures using high-resolution NMR spectroscopy without pre-installing metal chelators. Paramagnetic metals, such as Gd3+, appear to bind to the carboxyl groups of N-acetylneuraminic acid when introduced at room temperature, leading to the measurement of nonequivalent proton and carbon NMR spectral signals among otherwise "identical" glycan branched structures.
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