Multiple Choice
Which statement best supports the theory that primary protein structure dictates folding into its native state?
4. Protein Structure
Anfinsen Experiment
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Which of the following occurred when RNase A properly refolded from a denatured state?
A
The primary structure of the protein was rearranged.
B
Most of the charged, hydrophilic residues were found buried in the core of the protein.
C
The entropy of the protein structure itself was significantly increased.
D
None of the above.
Verified step by step guidance1
Understand that RNase A is a protein that can be denatured and then refolded to regain its native structure.
Recall that the primary structure of a protein, which is its sequence of amino acids, remains unchanged during denaturation and refolding. Denaturation affects the secondary, tertiary, and quaternary structures.
Recognize that in a properly folded protein, hydrophilic residues are typically found on the surface interacting with the aqueous environment, while hydrophobic residues are buried in the core. Thus, most charged, hydrophilic residues would not be buried in the core.
Consider the concept of entropy in protein folding. When a protein folds from a denatured state to its native state, the entropy of the protein itself decreases because it adopts a more ordered structure. However, the overall entropy of the system (protein plus solvent) may increase due to the release of water molecules from the protein's surface.
Conclude that none of the given statements accurately describe what occurs when RNase A properly refolds from a denatured state, as the primary structure remains unchanged, hydrophilic residues are not buried, and the protein's entropy decreases.
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