In sickle cell anemia, a hereditary disease, there is substitution of one amino acid by another in one of the four polypeptide chains of hemoglobin. In this case are all of the structural levels of the protein modified?
In sickle cell disease there is a change in the primary protein structure of one of the polypeptide chains that form hemoglobin: the amino acid glutamic acid is substituted by the amino acid valine in the β chain. The spatial conformation of the molecule in addition is also affected and modified by this primary “mistake” and the modification also creates a different (sickle) shape to the red blood cells. Modified, sickled, red blood cells sometimes aggregate and obstruct the peripheral circulation causing tissue hypoxia and the pain crisis typical of sickle cell anemia.
