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 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 α helices that are held together by disulfide bonds.
D) The protein is most likely composed of β sheets that are held together by disulfide bonds.
E) The primary and secondary structure of the protein depends on disulfide bonds.
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