Direct observation of glycans bonded to proteins and lipids at the single-molecule level
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Dokumenter
- Fulltext
Accepteret manuskript, 1,89 MB, PDF-dokument
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.
Originalsprog | Engelsk |
---|---|
Tidsskrift | Science (New York, N.Y.) |
Vol/bind | 382 |
Udgave nummer | 6667 |
Sider (fra-til) | 219-223 |
Antal sider | 5 |
ISSN | 0036-8075 |
DOI | |
Status | Udgivet - 2023 |
Antal downloads er baseret på statistik fra Google Scholar og www.ku.dk
Ingen data tilgængelig
ID: 381147304