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- W4387568586 abstract "Proteins and lipids decorated with glycans are found throughout biological entities, playing roles in biological functions and dysfunctions. Current analytical strategies for these glycan-decorated biomolecules, termed glycoconjugates, rely on ensemble-averaged methods that do not provide a full view of positions and structures of glycans attached at individual sites in a given molecule, especially for glycoproteins. We show single-molecule analysis of glycoconjugates by direct imaging of individual glycoconjugate molecules using low-temperature scanning tunneling microscopy. Intact glycoconjugate ions from electrospray are soft-landed on a surface for their direct single-molecule imaging. The submolecular imaging resolution corroborated by quantum mechanical modeling unveils whole structures and attachment sites of glycans in glycopeptides, glycolipids, N-glycoproteins, and O-glycoproteins densely decorated with glycans." @default.
- W4387568586 created "2023-10-13" @default.
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- W4387568586 date "2023-10-13" @default.
- W4387568586 modified "2023-10-14" @default.
- W4387568586 title "Direct observation of glycans bonded to proteins and lipids at the single-molecule level" @default.
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- W4387568586 doi "https://doi.org/10.1126/science.adh3856" @default.
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- W4387568586 hasPublicationYear "2023" @default.
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