The two polypeptides of human insulin are linked together by
- A.
Hydrogen bonds
- B.
Covalent bond
- C.
Disulphide bridges
- D.
Phosphodiester bond
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Background: human insulin is made up of two separate polypeptide chains, called the A-chain (21 amino acids) and the B-chain (30 amino acids), each held together internally by peptide bonds between amino acids.
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For the hormone to become fully functional, these two separate chains must be joined together through a special type of bond formed after the protein is made (a post-translational modification).
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This connection is achieved specifically through disulphide bridges, formed between cysteine residues — specifically linking positions A7 to B7, and A20 to B19.
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Hydrogen bonds and simple covalent bonds are too weak or too generic respectively to describe this specific, well-defined linkage, and a phosphodiester bond is the type of bond found in nucleic acid backbones (DNA/RNA), not in linking protein chains.
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Hence, the correct answer is C: Disulphide bridges.