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Sickle Cell Research Paper

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Sickle cell disease is caused by a seemingly negligible, but extremely life-threatening mutation in the patient’s hemoglobin protein.
Hemoglobin (Hb) is a specialized protein within red blood cells that can carry oxygen. This protein consists of four subunits: two alpha units and two beta units. Each subunit contains one ferrous ion that can reversibly bind to one oxygen molecule. Thus, one Hb protein can bind to a maximum of four oxygen molecules.
Red blood cells are specialized to contain as many Hb proteins as possible. When the blood with red blood cells flows to the lung, where oxygen concentration is relatively high, oxygen molecules can diffuse into the blood and bind to Hb proteins in the red blood cells. Then, when this oxygenated …show more content…
Even though they can still make Hb, the Hb they made (called HbS, S for sickle cell disease) is different from the normal one: on the beta subunit, a typically charged, polar part is changed to an uncharged, nonpolar block/stick. This seemingly trivial change will not cause a problem when HbS is oxygenated. However, when an Hb is deoxygenated, nonpolar, hydrophobic pockets, which are hidden when Hb is oxygenated, will be exposed on other subunits. (Both HbS and normal Hb have this pocket.) In this case, the block/stick can then fit into the pocket and two HbS proteins can aggregate together (like the south pole and north pole of two magnets, attracting each other). Later on, more and more HbS can aggregate and form long, complex fibers. These insoluble and strong fibers can distort the shape of red blood cells: from a round and flat shape to a long and sickle shape. These sickle cells have a much harder time flow through thin capillaries and may block local blood supply. Together with the dramatic decrease of oxygen binding ability of the fiber-form Hb, the sickle cells can cause oxygen & nutrients deficiency, which then leads to ischemic

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