Question

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 structure of the protein contains multiple cysteine residues that are hydeolyzed by chemical reluctant.
B) The protein is most likely composed of multiple polypeptide chains that are held together by disulfide bonds.
C) The protein is most likely composed of a helices that are held together by disulfide bonds.
D) The protein is most likely composed of beta sheets that are held together by disulfide bonds.
E) The primary and secondary structure of the protein depends on disulfide bonds

Answer 1

The correct answer is statement B.

Step-by-step explanation:

The enzymes may be present in the form of trimers, dimers, or tetramers. Various examples of trimers, dimers, and tetramer proteins are known, of them, the NEMO's diners are considered to be held by disulfide bonds. Thus, it can be hypothesized that the enzyme under examination is a multimer captivated by disulfide bonds, with each exhibiting catalytic sites.

On dissociation or reduction of disulfide bonds, the enzyme cleaves into its many single units. This illustrates the reduction in catalytic activity. Each active site in single unit will work, however, at a gradual rate. This also illustrates determination of multiple globular proteins after disulfide reduction.