Question

True/False: The use of mercaptoethanol to solubilize proteins involves disrupting disulfide bonds, leading to denaturation.

Answer 1

True. Mercaptoethanol, a reducing agent, disrupts disulfide bonds in proteins, causing their denaturation. This process involves breaking the covalent bonds that contribute to a protein's tertiary and quaternary structures, leading to the unfolding of the protein.

Answer 2

True. When mercaptoethanol is used to solubilize proteins, it disrupts disulfide bonds, leading to denaturation.

Step-by-step explanation:

True.

When mercaptoethanol is used to solubilize proteins, it disrupts disulfide bonds between cysteine residues in the protein structure. Disulfide bonds form when two cysteine residues come close together and form a covalent bond. By breaking these disulfide bonds, mercaptoethanol contributes to the denaturation of proteins, meaning it causes the protein to lose its three-dimensional structure and unfold.

For example, if we take a globular protein with disulfide bonds, adding mercaptoethanol would break those bonds, resulting in the denaturation of the protein. This denatured protein is no longer functional in its native state.