Denaturation disrupts the secondary and tertiary structure of proteins. However, denaturation is not strong enough to disrupt what interaction that is relevant to protein structure?
- Van der Waals attraction.
- Hydrophobic exclusion.
- Hydrogen bonds.
- Peptide bonds.
- lonic bonds.



Answer :

Answer: Peptide bonds

Explanation: Denaturation refers to the breakdown of protein structure due to abnormal temperature or pH levels. Denaturation breaks intermolecular forces such as hydrogen bonds, hydrophobic exclusion, and Van der Waals attraction. However, covalent bonds within a protein tend to remain intact even after denaturation due to their strength. The secondary and tertiary structure of proteins unravel after denaturation due to these structures relying on intermolecular forces to remain intact.

On the other hand, the peptide bonds that form the primary structure of a protein remain intact because they're covalent, making peptide bonds the right answer to the question.

Though ionic bonds are also strong enough to resist the effects of denaturation, they're not very relevant to the primary structure of the protein. They only play a role in tertiary structure, which is why ionic bonds is not the correct choice.