Multiple Choice
In general, which option contains the major cooperative interactions driving spontaneous protein folding?
4. Protein Structure
Protein Folding
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Which of the following occurs when myoglobin folds into its native conformation?
A
Myoglobin adopts its lowest energy state form.
B
Most of the nonpolar, hydrophobic amino acid residues are found buried in myoglobin's core.
C
Most polar, charged, hydrophilic residues are found on the outside of myoglobin.
D
b and c.
E
All the above.
Verified step by step guidance1
Understand the structure of myoglobin: Myoglobin is a globular protein primarily composed of alpha helices, as seen in the image. It functions in oxygen storage in muscle tissues.
Recognize the concept of protein folding: Proteins fold into their native conformation to achieve a stable, functional form. This involves adopting the lowest energy state, which is thermodynamically favorable.
Identify the distribution of amino acid residues: During folding, nonpolar, hydrophobic residues tend to be buried in the interior of the protein, away from the aqueous environment, while polar, charged, hydrophilic residues are exposed on the surface.
Analyze the image: The image shows myoglobin with its heme group, indicating the folded structure where hydrophobic residues are likely buried inside, and hydrophilic residues are on the surface.
Conclude based on the options: Given the understanding of protein folding and the image, all the statements provided (lowest energy state, hydrophobic core, hydrophilic surface) are correct for myoglobin's native conformation.
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