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Protein Glycosylation

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.
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Glycocalyx and its Functions

The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
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Oligosaccharide Assembly

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...

Proteoglycans

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,...

Glycosaminoglycans

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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.
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Related Experiment Video

Updated: Jun 21, 2026

Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals

Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals

Published on: February 14, 2019

Glycan arrays: recent advances and future challenges.

Oyindasola Oyelaran¹, Jeffrey C Gildersleeve

¹Laboratory of Medicinal Chemistry, Center for Cancer Research, National Cancer Institute/NIH, 376 Boyles Street, Frederick, MD 21702, USA.

Current Opinion in Chemical Biology

|July 24, 2009

Summary

Glycan arrays, tools for studying carbohydrate interactions, are advancing with new production methods. These carbohydrate arrays offer high-throughput analysis, significantly impacting glycobiology research and understanding macromolecule binding.

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Last Updated: Jun 21, 2026

Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals

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Area of Science:

Glycobiology
Carbohydrate Chemistry
Biotechnology

Background:

Carbohydrate arrays (glycan arrays) immobilize diverse carbohydrates on solid supports.
This technology enables high-throughput analysis of carbohydrate-macromolecule interactions.
Glycan arrays have become instrumental in advancing glycobiology research.

Purpose of the Study:

To review recent advancements in glycan array technology.
To identify limitations and opportunities for improving glycan array applications.
To highlight new methods for glycan array production and their impact.

Main Methods:

Review of recent literature on glycan array technology.
Focus on new methods for producing natural glycan arrays.
Discussion of chemoenzymatic approaches for expanding structural diversity.

Main Results:

New production methods are significantly increasing the diversity of structures available on glycan arrays.
Chemoenzymatic approaches are crucial for generating complex and varied carbohydrate structures.
Understanding and controlling carbohydrate presentation is key to enhancing binding interactions.

Conclusions:

Recent advances in glycan array production are expanding their utility in glycobiology.
Further development is needed to address limitations and optimize carbohydrate presentation.
Glycan array technology holds significant promise for future discoveries in molecular interactions.