Answer:
The correct answer is option B. The tertiary structure of the beta subunit changes, exposing a hydrophobic cleft which allows hemoglobin to form long chains in RBC.
Step-by-step explanation:
As it is clearly mention as there is point mutation that leads to single nucleotide change which results in to valine instead of glutamate. Valine is hydrophobic in nature not like glutamate. Valine aggregate and makes a rigid structure of molecules.
Due to this rigid molecule of valine aggregates, RBCs form a crescent or sickle like shape due to the higher viscosity and low solubility of Mutated hemoglobin in deoxy condition. It leads to formation of polymer that blocks the vessels.
Thus, the correct answer is option B.