Multiple Choice
Which of the following conclusions could Anfinsen draw from his RNase A experiment?
4. Protein Structure
Anfinsen Experiment
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Which statement best supports the theory that primary protein structure dictates folding into its native state?
A
RNase A loses all enzymatic activity upon denaturing in 8M urea.
B
RNase A regains enzymatic activity upon removing urea & β-ME.
C
Purified RNase A has 100% enzymatic activity in vitro.
D
A reducing agent such as β-ME destroys disulfide bonds & eliminates RNase A enzymatic activity.
Verified step by step guidance1
Understand that the primary structure of a protein refers to its sequence of amino acids. This sequence determines how the protein will fold into its three-dimensional structure, which is crucial for its function.
Recognize that denaturation involves the unfolding of a protein, leading to the loss of its functional three-dimensional structure and, consequently, its activity.
Consider the role of urea and β-mercaptoethanol (β-ME) in denaturation: urea disrupts hydrogen bonds, while β-ME reduces disulfide bonds, both of which are important for maintaining the protein's structure.
Analyze the statement that RNase A regains enzymatic activity upon removing urea and β-ME. This suggests that the protein can refold into its native, functional state once the denaturing agents are removed, indicating that the primary structure contains all the necessary information for correct folding.
Conclude that the ability of RNase A to regain activity after the removal of denaturing agents supports the theory that the primary structure dictates the folding and final functional form of the protein.
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