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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...

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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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Harnessing glycomics technologies: integrating structure with function for glycan characterization.

Luke N Robinson1, Charlermchai Artpradit, Rahul Raman

  • 1Department of Biological Engineering, Harvard-MIT Division of Health Sciences & Technology and Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA, USA.

Electrophoresis
|April 24, 2012
PubMed
Summary
This summary is machine-generated.

Glycans, or complex carbohydrates, are vital for many biological processes. This study details glycomics technologies to characterize acidic glycans, enabling robust structure-function relationship development.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Glycoscience
  • Carbohydrate Chemistry

Background:

  • Glycans (complex carbohydrates) are crucial for diverse physiological processes, including cell signaling, development, and pathogenesis.
  • Studying glycans is challenging due to their complex structures and the importance of multivalency in biological interactions.
  • Decoding glycan structure-function relationships requires integrating information from multiple complementary methods.

Purpose of the Study:

  • To describe key glycomics technologies for characterizing acidic glycans.
  • To elucidate the role of acidic glycans in biological processes.
  • To highlight the integration of orthogonal data for glycan characterization.

Main Methods:

  • Glycomics technologies for structural attribute characterization (linkage, modifications, topology).
  • Case studies involving sialylated branched glycans and sulfated glycosaminoglycans.
  • Integration of diverse datasets from orthogonal methods.

Main Results:

  • Demonstrated key glycomics technologies for detailed acidic glycan structural analysis.
  • Illustrated the application of these technologies in two distinct glycan classes.
  • Showcased how integrating orthogonal data accelerates glycan characterization.

Conclusions:

  • Integrated glycomics approaches are essential for robustly defining glycan structure-function relationships.
  • Characterization of acidic glycans, including sialylated and sulfated types, benefits from multi-platform data integration.
  • This work provides a framework for advancing glycomics research and understanding biological roles of glycans.