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Glycan and Post-translational modification

Shortcuts: Differences, Similarities, Jaccard Similarity Coefficient, References.

Difference between Glycan and Post-translational modification

Glycan vs. Post-translational modification

The terms glycan and polysaccharide are defined by IUPAC as synonyms meaning "compounds consisting of a large number of monosaccharides linked glycosidically". Post-translational modification (PTM) refers to the covalent and generally enzymatic modification of proteins following protein biosynthesis.

Similarities between Glycan and Post-translational modification

Glycan and Post-translational modification have 14 things in common (in Unionpedia): Asparagine, Carbohydrate, Cell membrane, Cysteine, Enzyme, Eukaryote, Glycan, Glycoprotein, Glycosylation, Glycosylphosphatidylinositol, Mass spectrometry, Proline, Serine, Threonine.

Asparagine

Asparagine (symbol Asn or N), is an α-amino acid that is used in the biosynthesis of proteins.

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Carbohydrate

A carbohydrate is a biomolecule consisting of carbon (C), hydrogen (H) and oxygen (O) atoms, usually with a hydrogen–oxygen atom ratio of 2:1 (as in water); in other words, with the empirical formula (where m may be different from n).

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Cell membrane

The cell membrane (also known as the plasma membrane or cytoplasmic membrane, and historically referred to as the plasmalemma) is a biological membrane that separates the interior of all cells from the outside environment (the extracellular space).

Cell membrane and Glycan · Cell membrane and Post-translational modification · See more »

Cysteine

Cysteine (symbol Cys or C) is a semi-essential proteinogenic amino acid with the formula HO2CCH(NH2)CH2SH.

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Enzyme

Enzymes are macromolecular biological catalysts.

Enzyme and Glycan · Enzyme and Post-translational modification · See more »

Eukaryote

Eukaryotes are organisms whose cells have a nucleus enclosed within membranes, unlike Prokaryotes (Bacteria and other Archaea).

Eukaryote and Glycan · Eukaryote and Post-translational modification · See more »

Glycan

The terms glycan and polysaccharide are defined by IUPAC as synonyms meaning "compounds consisting of a large number of monosaccharides linked glycosidically".

Glycan and Glycan · Glycan and Post-translational modification · See more »

Glycoprotein

Glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to amino acid side-chains.

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Glycosylation

Glycosylation (see also chemical glycosylation) is the reaction in which a carbohydrate, i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule (a glycosyl acceptor).

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Glycosylphosphatidylinositol

Glycosylphosphatidylinositol, or glycophosphatidylinositol, or GPI in short, is a glycolipid that can be attached to the C-terminus of a protein during posttranslational modification.

Glycan and Glycosylphosphatidylinositol · Glycosylphosphatidylinositol and Post-translational modification · See more »

Mass spectrometry

Mass spectrometry (MS) is an analytical technique that ionizes chemical species and sorts the ions based on their mass-to-charge ratio.

Glycan and Mass spectrometry · Mass spectrometry and Post-translational modification · See more »

Proline

Proline (symbol Pro or P) is a proteinogenic amino acid that is used in the biosynthesis of proteins.

Glycan and Proline · Post-translational modification and Proline · See more »

Serine

Serine (symbol Ser or S) is an ɑ-amino acid that is used in the biosynthesis of proteins.

Glycan and Serine · Post-translational modification and Serine · See more »

Threonine

Threonine (symbol Thr or T) is an amino acid that is used in the biosynthesis of proteins.

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The list above answers the following questions

Glycan and Post-translational modification Comparison

Glycan has 90 relations, while Post-translational modification has 170. As they have in common 14, the Jaccard index is 5.38% = 14 / (90 + 170).

References

This article shows the relationship between Glycan and Post-translational modification. To access each article from which the information was extracted, please visit:

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