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Related Concept Videos

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,...
Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan biosynthesis begins in...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
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...
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...

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Related Experiment Video

Updated: May 23, 2026

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
14:02

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry

Published on: April 21, 2017

Proteoglycan sequence.

Lingyun Li1, Mellisa Ly, Robert J Linhardt

  • 1Departments of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.

Molecular Biosystems
|April 20, 2012
PubMed
Summary
This summary is machine-generated.

Sequencing glycosaminoglycan (GAG) chains in proteoglycans (PGs) is challenging. Recent advances in glycomics and mass spectrometry offer new insights into GAG sequencing for understanding PGs in development and disease.

More Related Videos

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

Related Experiment Videos

Last Updated: May 23, 2026

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
14:02

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry

Published on: April 21, 2017

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

Area of Science:

  • Biochemistry
  • Glycobiology
  • Proteomics

Background:

  • Proteoglycans (PGs) are complex biomacromolecules essential for animal cell functions, mediating interactions via protein ligands and receptors.
  • PGs consist of a core protein with attached glycosaminoglycan (GAG) chains, whose biosynthesis and structure are not fully understood.
  • While protein sequencing is routine, GAG chain sequencing remains a significant challenge due to underdeveloped glycomics.

Purpose of the Study:

  • To review recent advancements in sequencing glycosaminoglycan (GAG) chains over the past decade.
  • To highlight the challenges in sequencing complex proteoglycans (PGs).
  • To discuss the implications of GAG sequencing for understanding PGs in developmental biology and pathogenesis.

Main Methods:

  • Review of literature on glycomics and mass spectrometry techniques.
  • Analysis of Fourier transform mass spectral data for GAG chain sequencing.
  • Examination of proteomic and molecular biology approaches for protein core sequencing.

Main Results:

  • Recent studies suggest defined sequences for GAG chains, evidenced by Fourier transform mass spectral data.
  • Significant progress has been made in glycomics, improving the ability to analyze GAG structures.
  • The complexity of PGs and their biosynthesis pathways continue to present challenges for complete sequencing.

Conclusions:

  • Advances in mass spectrometry and glycomics are improving the sequencing of GAG chains.
  • Accurate GAG sequencing is crucial for understanding the biological roles of complex PGs.
  • Further research is needed to overcome challenges in GAG sequencing for applications in developmental biology and disease pathogenesis.