You are researching a cytoplasmic protein associated with a nerve disorder. The native form of the enzyme appears to be globular protein; however, when a sample of the purified protein is treated with a chemical that reduces disulfide bonds, the enzymatic activity decreases dramatically and multiple globular proteins can be detected in the sample. What does this tell you about the protein?a. The primary and secondary structure of the protein depends on disulfide bonds.
b. The protein is most likely composed of \alpha helices that are held together by disulfide bonds.
c. The protein is most likely composed of \betha sheets that are held together by disulfide bonds.
d. The primary structure of the protein contains multiple cysteine residues that are hydrolyzed by the chemical reductant.
e. The protein is most likely composed of multiple polypeptide chains that are held together by disulfide bonds.

e. The protein is most likely composed of multiple polypeptide chains that are held together by disulfide bonds.

Explanation:

The disuplhide bond is formed between two thiol groups of cysteine residues in proteins. The disulphide linkages are found between secondary, tertiary and quaternary structure of protein.

Let us discuss the protein in example now;

The native form of the enzyme appears to be globular protein indicates that protein either have tertiary or quternary structure. Primary and secondary srtucture can't have globular protein.

when a sample of the purified protein is treated with a chemical that reduces disulfide bonds, the enzymatic activity decreases dramatically and multiple globular proteins can be detected in the sample indicates that proteins have Quaternary structure because quaternary structure comprises of more than one polypeptide chain and each polypeptide can exhibit globular structure.

That why we can say The protein is most likely composed of multiple polypeptide chains (quaternary structure) that are held together by disulfide bonds.

thinking it would be d not too sure but i think it's right