Which intermolecular interaction is being disrupted when a protein is denatured
using heavy metals?
disulfide bonds
hydrophobic interactions
none of these answers are correct
hydrogen bonds



Answer :

When a protein is denatured using heavy metals, the intermolecular interaction that is being disrupted is the disulfide bonds. Disulfide bonds are covalent bonds that form between the sulfur atoms of cysteine residues in a protein. These bonds help stabilize the protein's tertiary structure. When heavy metals interact with proteins, they can bind to the sulfur atoms of the cysteine residues, breaking the disulfide bonds. This disruption leads to the unfolding and misfolding of the protein, ultimately causing denaturation. In this case, the correct answer is disulfide bonds.