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Protein Function and the Bohr Effect

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PROTEIN FUNCTION-MYOGLOBIN AND HEMOGLOBIN
208.5.3-01-05
Hemoglobin Model
Comparison to Oxygenated and Deoxygenated Hemoglobin
The Bohr Effect
* The Bohr effect is the relationship between hemoglobin and pH’s ability to bind oxygen. I will explain this in more detail. We begin our journey in the lungs. Our lungs have the most amount of oxygen in the body. This is a good thing because our hemoglobin is strongly attracted to and has a high affinity to oxygen. The oxygen gets heavily bound to the hemoglobin and this helps to deliver the oxygen to rest of the body. The Bohr effect allows the steady release of this bound up oxygen throughout the body while the blood is delivered to the other parts of the body such as the fingers and toes. You see our pH in the lungs is around 7.4. As the blood moves through our body our pH is changed to around 7.2 because the blood picks up carbon dioxide. Carbon dioxide is produced by our cells in the citric acid cycle and each round of the citric acid cycle causes our carbon dioxide to increase. Each cell performs this citric acid cycle, which causes a lot of carbon dioxide to build up. Our blood picks the carbon dioxide up to be able to bring it back to the lungs to be blown out of the body, but as the blood is picking up carbon dioxide it is also leaving the oxygen it needs from the blood. You see the Boher effect allows this to happen.

Bohr Effect Graph
Hemoglobin vs. Myoglobin
Sickle Cell Anemia (amino acid) Diagram
Sickle Cell Anemia (cellular level)
Sickle Cell Anemia
* The normal red blood cell is round and concave in the middle. The sickle cell red blood cell is long and elongated and they become sticky and get stuck in the small veins. This happens due to a single amino acid change. The amino acid change is from the regular glutamie acid to the mutation of valine. The valine is on the surface of the hemoglobin and

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