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Post-translational Modification and Collagen Biosynthesis Quiz
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Which statement best describes glycosylation as a post-translational modification?
- A Reversible addition of a phosphate group to serine, threonine or tyrosine residues You picked ✕
- B Non-covalent binding of sugars to proteins to stabilise tertiary structure You picked ✕
- C Proteolytic cleavage of a precursor protein to form an active product You picked ✕
- D Attachment of lipid molecules to proteins to anchor them in cell membranes You picked ✕
- E Covalent attachment of a carbohydrate group to a protein after it has been synthesised You picked ✓
Correct!
Incorrect
The answer is E: Covalent attachment of a carbohydrate group to a protein after it has been synthesised
Explanation
Why E is correct
See Glycosylation. Option E is correct. Post-translational modification means a chemical change made to a protein after it has been built by translation. Glycosylation is one of the most common: an enzyme covalently attaches a carbohydrate, in the form of a sugar or a short chain of sugars (a glycosyl group), to a protein, forming a glycosidic bond (a bond that links a sugar to another molecule). It needs many enzymes and steps, and is under strict enzymatic control. There are two main types. In N-linked glycosylation, which takes place in the endoplasmic reticulum, the sugar is attached to the nitrogen atom of an asparagine residue. In O-linked glycosylation, which takes place in the Golgi apparatus, it is attached to the hydroxyl group of serine or threonine. Glycosylation helps proteins to fold correctly, makes them more stable and affects how they interact with other molecules. Do not confuse it with glycation, in which a sugar such as glucose attaches to a protein without an enzyme, as in glycated haemoglobin (HbA1c).
- Definition: glycosylation is the covalent attachment of a carbohydrate to a protein after it has been made.
- Types: N-linked glycosylation occurs in the ER on asparagine, and O-linked glycosylation occurs in the Golgi on serine or threonine.
- Contrast: glycation is non-enzymatic, as in glycated haemoglobin (HbA1c).
Why the other options are incorrect
- A. Reversible addition of a phosphate group to serine, threonine or tyrosine residues: This describes phosphorylation, in which a kinase adds a phosphate group to serine, threonine or tyrosine. It is reversible and mainly regulates activity, whereas glycosylation attaches carbohydrate. Your answer
- B. Non-covalent binding of sugars to proteins to stabilise tertiary structure: Glycosylation forms covalent bonds, and the sugars are attached by enzymes, so non-covalent binding of sugars does not describe it. The non-enzymatic attachment of sugar to proteins is called glycation. Your answer
- C. Proteolytic cleavage of a precursor protein to form an active product: Proteolytic cleavage cuts a precursor protein into its active form, for example the processing of insulin. It removes pieces and does not attach sugars. Your answer
- D. Attachment of lipid molecules to proteins to anchor them in cell membranes: Attaching lipid molecules to anchor proteins in membranes is a different modification. Glycosylation attaches carbohydrate, not lipid. Your answer
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More questions from this set. Start the quiz to answer them and see each explanation.
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1
Which statement best describes the purpose of proteolytic cleavage in protein processing?
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2
Which feature of collagen’s molecular structure most directly allows the three polypeptide chains to pack tightly into a stable triple helix?
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