Home › AP Biology › Biology › Biological Macromolecules › Denaturation is often reversible because the pro…
Denaturation is often reversible because the process leaves intact the protein's:
APrimary structure
BTertiary structure
CSecondary structure
DQuaternary structure
Answer & Solution
Correct answer: A. Primary structure
1. Heat, pH change or chemical exposure can make a protein lose its three-dimensional shape.
2. That loss of shape without loss of the underlying sequence is denaturation.
3. The primary structure of the polypeptide is conserved in the process.
4. So when the denaturing agent is removed the chain can refold and resume its function.
5. The secondary, tertiary and quaternary levels are exactly the levels that are lost, so none of them can be the answer.
_Source: OpenStax Biology for AP(R) Courses (CC BY 4.0), Ch 3 'Biological Macromolecules', sections 3.1-3.5_
Related questions
In the sugar-phosphate backbone of a nucleic acid, the phosphate residue links:In the alpha helix, a hydrogen bond forms between the carbonyl oxygen of one amino acid anSickle cell disease arises from a change in hemoglobin at:Nine of the twenty amino acids are called essential in humans because they:A fatty acid is named omega-3 when the:Termites can survive on wood because they:Cellulose and starch are both glucose polymers, yet humans digest only starch. The structuBases in nucleic acids fall into two categories. Cytosine, thymine and uracil are: