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In the structure of pro - insulin in hum...

In the structure of pro - insulin in humans disulphide bonds exist between

A

between B peptide and C peptide

B

between A peptide and B peptide

C

between C peptide and A peptide

D

between A and C peptide as well as B and C peptide

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To solve the question regarding the structure of pro-insulin in humans and the existence of disulfide bonds, we can follow these steps: ### Step-by-Step Solution: 1. **Understanding Pro-insulin Structure**: - Pro-insulin is a precursor molecule to insulin, consisting of three peptide chains: the A-peptide, B-peptide, and C-peptide. 2. **Identifying Peptide Chains**: - The A-peptide and B-peptide are the two chains that will eventually form the active insulin molecule after the C-peptide is removed. 3. **Role of Disulfide Bonds**: - Disulfide bonds are covalent bonds that form between the sulfur atoms of cysteine residues in proteins. They play a crucial role in stabilizing the three-dimensional structure of proteins. 4. **Locating Disulfide Bonds in Pro-insulin**: - In pro-insulin, disulfide bonds are specifically formed between the A-peptide and B-peptide. This bonding is essential for the proper folding and stability of the insulin molecule. 5. **Final Confirmation**: - Upon the cleavage of the C-peptide, the A-peptide and B-peptide remain connected by these disulfide bonds, forming the functional insulin molecule. ### Conclusion: - Therefore, in the structure of pro-insulin in humans, disulfide bonds exist between the A-peptide and B-peptide.
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