In 1956, Vernon Ingram mapped out the amino acid sequence of sickle hemoglobin, and showed that there was only ONE amino acid difference -- a glutamic acid at position 6 is replaced by a valine on the beta globin chain. This made sickle cell disease the first known genetic disorder.
This change of position results in the protein becoming more hydrophobic.
Instead of the positive (?) radical Alanine (CH3), Glutamine has strong negative charge! The whole hemoglobin will not move as fast through the magnetized field in electrophoresis.What difference could this make in such a large molecule as hemoglobin?
Read more on variations in hemoglobin and Sickle Cell
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