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Protein Structure: Hemoglobin and Sickle-Cell Anemia

APBIO-KL4HKE

Hemoglobin is a protein used by humans to carry oxygen in the blood. It is composed of four polypeptide subunits (two alpha and two beta subunits).

Sickle cell anemia is a disease caused by a genetic mutation that results in the amino acid valine being incorporated instead of glutamic acid at a particular position in the polypeptide chain of the beta subunits.

The consequence is that the hemoglobin proteins in people suffering from sickle cell anemia fold in such a way that their ability to carry oxygen is drastically reduced.

Based on this information, we can conclude that sick-cell hemoglobin proteins display

A

altered primary and secondary structure but not tertiary or quaternary structure.

B

altered primary and tertiary structure but not secondary or quaternary structure.

C

altered tertiary and quaternary structure but not primary or secondary structure.

D

altered primary, secondary, tertiary and quaternary structure.