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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...
Glycosaminoglycans01:23

Glycosaminoglycans

Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
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,...
Nucleic Acid Structure01:25

Nucleic Acid Structure

The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA has a double-helix structure. The...

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Related Experiment Video

Updated: May 22, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

N-glycopedia: libraries for native N-glycan structural analysis.

Christopher Ashwood1,2,3, Richard D Cummings4

  • 1Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.

Nature Communications
|May 20, 2026
PubMed
Summary
This summary is machine-generated.

This study introduces an N-glycopedia, a valuable resource for glycomics research. It provides high-resolution data for 226 N-glycan standards, aiding in structural characterization.

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Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+
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Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+

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Last Updated: May 22, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+
08:26

Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+

Published on: June 25, 2018

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Glycomics

Background:

  • Glycoprotein glycan analysis is challenging due to structural diversity.
  • A lack of comprehensive N-glycan standards limits accurate characterization.

Purpose of the Study:

  • To develop a high-resolution method for N-glycan separation and characterization.
  • To create a publicly accessible N-glycan database (N-glycopedia) for glycomics research.

Main Methods:

  • Utilized a library of 226 diverse N-glycan standards.
  • Employed porous graphitized carbon liquid chromatography-mass spectrometry (PGC-LC-MS).
  • Generated retention time data, diagnostic fragments, and validated structural assignments.

Main Results:

  • Achieved high-resolution separation and characterization of underivatized N-glycans.
  • Established a comprehensive N-glycopedia with validated glycan data.
  • The developed platform supports both targeted and discovery-based glycomics.

Conclusions:

  • The N-glycopedia serves as a robust reference for N-glycan structural analysis.
  • This method overcomes limitations of compositional data and predicted structures.
  • The technology is scalable for future inclusion of new N-glycan standards.