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  2. N-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/N-linked_glycosylation

    The different types of lipid-linked oligosaccharide (LLO) precursor produced in different organisms.. N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in ...

  3. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    N-linked glycosylation is a very prevalent form of glycosylation and is important for the folding of many eukaryotic glycoproteins and for cell–cell and cell–extracellular matrix attachment. The N-linked glycosylation process occurs in eukaryotes in the lumen of the endoplasmic reticulum and widely in archaea, but very rarely in bacteria.

  4. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    The most common method of glycosylation of N-linked glycoproteins is through the reaction between a protected glycan and a protected Asparagine. [5] Similarly, an O-linked glycoprotein can be formed through the addition of a glycosyl donor with a protected Serine or Threonine. [5] These two methods are examples of natural linkage. [5]

  5. O-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/O-linked_glycosylation

    O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O -glycosylation is a post-translational modification that occurs after the protein has been synthesised.

  6. Oligosaccharide - Wikipedia

    en.wikipedia.org/wiki/Oligosaccharide

    The process of N-linked glycosylation occurs cotranslationally, or concurrently while the proteins are being translated. Since it is added cotranslationally, it is believed that N -linked glycosylation helps determine the folding of polypeptides due to the hydrophilic nature of sugars.

  7. Protein biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Protein_biosynthesis

    N-linked glycosylation starts in the endoplasmic reticulum with the addition of a precursor glycan. The precursor glycan is modified in the Golgi apparatus to produce complex glycan bound covalently to the nitrogen in an asparagine amino acid. In contrast, O-linked glycosylation is the sequential covalent addition of individual sugars onto the ...

  8. Oligosaccharyltransferase - Wikipedia

    en.wikipedia.org/wiki/Oligosaccharyltransferase

    The sugar Glc 3 Man 9 GlcNAc 2 (where Glc=Glucose, Man=Mannose, and GlcNAc=N-acetylglucosamine) is attached to an asparagine (Asn) residue in the sequence Asn-X-Ser or Asn-X-Thr where X is any amino acid except proline. This sequence is called a glycosylation sequon. The reaction catalyzed by OST is the central step in the N-linked ...

  9. Post-translational modification - Wikipedia

    en.wikipedia.org/wiki/Post-translational...

    N-acetylation (N-terminus), N-linked ubiquitination, oxidation to sulfoxide or sulfone: Phenylalanine: Phe or F Proline: Pro or P hydroxylation: Serine: Ser or S phosphorylation, O-linked glycosylation, N-acetylation (N-terminus) Threonine: Thr or T phosphorylation, O-linked glycosylation, N-acetylation (N-terminus) Tryptophan: Trp or W