ArticleChembiochem : a European journal of chemical biology2022
Determination of Amide cis/trans Isomers in N-Acetyl-d-glucosamine: Tailored NMR Analysis of the N-Acetyl Group Conformation.
Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Theoretical Study of the Influence of K20N Glycosylation on the Dynamic Behavior of Im7 Protein.Molecules (Basel, Switzerland) · 2025Article
- Effectively alleviate rheumatoid arthritis via maintaining redox balance, inducing macrophage repolarization and restoring homeostasis of fibroblast-like synoviocytes by metformin-derived carbon dots.Journal of nanobiotechnology · 2025Article
- Primary Structure of Glycans by NMR Spectroscopy.Chemical reviews · 2023Review
- Integration of LC-MS-Based and GC-MS-Based Metabolic Profiling to Reveal the Effects of Domestication and Boiling on the Composition of Duck Egg Yolks.Metabolites · 2023Article
- Determination of Amide cis/trans Isomers in N-Acetyl-d-glucosamine: Tailored NMR Analysis of the N-Acetyl Group Conformation.Chembiochem : a European journal of chemical biology · 2022Article
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Abstract
N-Acetyl-d-glucosamine (GlcNAc) is one of the most common amino sugars in nature, but the conformation of its N-acetyl group has drawn little attention. We report herein the first identification of NH protons of the amide cis forms of α- and β-GlcNAc by NMR spectroscopy. Relative quantification and thermodynamic analysis of both cis and trans forms was carried out in aqueous solution. The NH protons were further utilized by adapting protein NMR experiments to measure eight J-couplings within the N-acetyl group, of which six are sensitive to the H2-NH conformation and two are sensitive to the amide conformation. For amide cis and trans forms, the orientation between H2 and NH was determined as anti conformation, while a small percentage of syn conformation was predicted for the amide trans form of β-GlcNAc. This approach holds great promise for the detailed conformational analysis of GlcNAc in larger biomolecules, such as glycoproteins and polysaccharides.
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