Question

You are researching an enzymatic protein in the lab and make the following observations. The usual form of the protein is globular (spherical) however, when a sample of the protein is treated with a chemical that reduces disulfide bonds, the rate of enzymatically driven product formation decreases dramatically and multiple globular proteins can be detected in the sample. From these observations you conclude: A. The primary structure of the protein contains multiple cysteine residues that are hydrolyzed by the chemical reductant. 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 primary and secondary structure of the protein depends on disulfide bonds. E. None of the provided statements are reasonable conclusions based on the observations,

Answer 1

Option B

Step-by-step explanation:

Since the usual shape of the protein is supposed to be globular and even after treatment, it still produces the same globular proteins despite the reduction of its disulphide bonds.

The disulphide bonds should have disrupted the shape formation if it had been a mechanism for its shape formation but since multiple globular polypeptide resulted from the treatment it can be assumed that the multiple polypeptide chains are held together by disulfide bonds which are hydrolyzed by the chemical.

Answer 2

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

Step-by-step explanation:

The Disulfide bonds in protein membranes are usually seen in bacteria and eukaryotes.