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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.
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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Proteoglycans01:05

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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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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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A Boltzmann model predicts glycan structures from lectin binding.

Aria Yom1, Austin Chiang2,3,4, Nathan E Lewis5,2

  • 1Department of Physics, University of California, San Diego. CA 92093, USA.

Biorxiv : the Preprint Server for Biology
|June 19, 2023
PubMed
Summary
This summary is machine-generated.

This study introduces a new method for glycan sequencing using lectin binding data. A Boltzmann model accurately predicts glycan structures, simplifying glycoprotein research and glycobiology applications.

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Computational Biology

Background:

  • Glycans (complex oligosaccharides) play crucial roles in biological processes and diseases.
  • Current glycan sequencing methods are time-consuming and require specialized expertise.
  • Efficient glycan analysis is vital for understanding biological functions and disease mechanisms.

Conclusions:

  • Lectin binding fingerprints combined with a Boltzmann model offer a feasible and accurate approach for glycan sequencing.
  • This method has the potential to significantly simplify and accelerate glycoprotein research.
  • The findings provide valuable insights for researchers utilizing lectins in glycobiology studies.