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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

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Related Experiment Video

Updated: May 19, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

Protein O-glycosylation analysis.

Gerhild Zauner1, Radoslaw P Kozak, Richard A Gardner

  • 1Biomolecular Mass Spectrometry Unit, Department of Parasitology, Leiden University Medical Center, P.O. Box 9600, NL-2300 RC Leiden, The Netherlands.

Biological Chemistry
|September 5, 2012
PubMed
Summary
This summary is machine-generated.

This review covers methods for analyzing O-glycosylation, focusing on released glycans, glycopeptides, and MS fragmentation techniques for O-glycan analysis.

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The Application of Open Searching-based Approaches for the Identification of Acinetobacter baumannii O-linked Glycopeptides

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Glycobiology

Background:

  • O-glycosylation is a crucial post-translational modification impacting protein function.
  • Comprehensive analysis of O-glycans is essential for understanding biological processes.
  • Existing analytical methods present challenges in sensitivity and specificity.

Purpose of the Study:

  • To provide a comprehensive overview of current O-glycosylation analysis methods.
  • To highlight the strengths and limitations of different analytical approaches.
  • To discuss future challenges in the field of O-glycan analysis.

Main Methods:

  • Analysis of released O-glycans: liberation, derivatization, and detection.
  • Analysis of O-glycosylated peptides for site identification.
  • Mass spectrometry (MS) fragmentation techniques: CID, ECD, ETD for O-glycopeptide analysis.

Main Results:

  • Detailed comparison of methods for analyzing released O-glycans.
  • Evaluation of peptide-based approaches for mapping O-glycosylation sites.
  • In-depth discussion of MS fragmentation techniques for O-glycopeptide characterization.

Conclusions:

  • O-glycopeptide analysis offers the most comprehensive information but remains the most challenging.
  • Advancements in MS fragmentation techniques are critical for detailed O-glycan analysis.
  • Addressing current analytical challenges is key to advancing O-glycosylation research.