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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.
Glycosylation occurs in...

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...

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,...

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Related Experiment Video

Updated: Mar 10, 2026

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments

Published on: February 7, 2025

Chemical Glycoproteomics.

Krishnan K Palaniappan¹, Carolyn R Bertozzi

¹Verily Life Sciences , 269 East Grand Ave., South San Francisco, California 94080, United States.

Chemical Reviews

|December 15, 2016

Summary

This summary is machine-generated.

Chemical glycoproteomics advances protein glycosylation research. These methods identify glycosylation sites and structures, aiding the characterization of the human glycoproteome and protein function studies.

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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Area of Science:

Glycoscience
Biochemistry
Proteomics

Background:

Protein glycosylation is a widespread and complex posttranslational modification crucial for biological processes.
Studying protein glycosylation has been experimentally challenging.
Chemical tools and mass spectrometry have significantly advanced glycoscience.

Purpose of the Study:

To review the role of chemical glycoproteomics in advancing the study of protein glycosylation.
To summarize key developments in chemical glycoproteomics methods.
To provide a foundation for future technological advancements in the field.

Main Methods:

Enrichment of glycoproteins and glycopeptides using chemical properties or metabolic labeling.
Chemoenzymatic tagging for introducing unnatural functional groups.
Identification of glycosylation sites and glycan structures.
Targeted and functional glycoproteomics approaches.

Main Results:

Chemical glycoproteomics enables identification of specific glycosylation sites and glycan structures.
These methods are crucial for understanding how glycosylation modulates protein function.
Technological advancements are paving the way for full human glycoproteome characterization.

Conclusions:

Chemical glycoproteomics is a rapidly growing field with significant impact on glycoscience.
Continued innovation in chemical methods and mass spectrometry will drive further exploration of protein glycosylation.
These advancements are essential for understanding diverse biological processes regulated by protein glycosylation.