Protein Glycosylation

Protein glycosylation methods article

By Jared Snider

We are proud to present a new article on protein glycosylation and methods to detect and analyze glycoproteins and glycopeptides, respectively. This article is the most recent addition to the series on post-translational modifications in the Protein Methods Library.

Glycosylation is a common post-translational modification that links proteins to sugars to generate broad proteomic diversity. Glycoproteins are critical for protein-protein interactions in the cell and cell attachment to the extracellular matrix and to other cells. Proteins can be glycosylated via different mechanisms, including N-, O- and C-linked glycosylation and phosphoglycosylation. Furthermore, various glycans (oligosaccharides) can be attached to proteins, such as high-mannose and complex oligosaccharides and GPI anchors.

Methods to detect glycoproteins vary, although most of them depend on chemical derivation of carbohydrates to form reactive aldehydes, which can then be directly stained or crosslinked to tags for detection or purification. Additionally, glycoproteins can be digested into glycopeptides and identified or quantitated by mass spectrometry (MS).

Topics discussed include:

  • Glycan staining and labeling
  • Glycoprotein purification/enrichment
  • Glycoproteome and glycome analysis
  • Overviews of N-, O- and C-glycosylation, glypiation (GPI anchor) and phosphoglycosylation.

Read the Article:

Protein Glycosylation

Protein Glycosylation