Chemistry Question 68 – JEE-MAIN 2026
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The tertiary structure of a protein is its overall three-dimensional shape, formed by the folding of secondary structures. It is stabilized by various interactions between the R-groups of amino acids, including hydrogen bonds, ionic bonds (electrostatic forces), hydrophobic interactions (van der Waals forces), and covalent disulfide bridges.
Changes in pH affect the ionization state of acidic and basic amino acid side chains. This alters the charges on these groups, thereby disrupting the ionic bonds and hydrogen bonds that are crucial for maintaining the specific three-dimensional conformation of the tertiary structure. Extreme pH values can lead to denaturation, where the protein loses its native structure and biological activity.
Remember that ionic and hydrogen bonds are sensitive to changes in proton concentration.
Based on the analysis, the statement 'The structure remains intact when exposed to pH changes' is incorrect. pH changes cause alterations in the stabilizing forces, leading to the disruption of the tertiary structure (denaturation).
Review the conditions that cause protein denaturation, such as extreme pH, temperature, and certain chemicals.
