Myoglobin/Hemoglobin Essay

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PROTEIN FUNCTION MYOGLOBIN AND HEMOGLOBIN Model of how oxygen is carried by hemoglobin The major differences in oxygenated and deoxygenated states of hemoglobin Oxygenated: Heme is planar configured, in a R (relaxed) state. Bound to oxygen gives a bright red color. Deoxygenated: Heme is dome configured, in a T (tense) state. Color is not bright. Hudon-Miller, S. (2012). Description of the Bohr Effect for the association and disassociation of oxygen and hemoglobin The Bohr Effect is the relationship between pH (measurement of hydronium concentration of a solution) and hemoglobin’s ability to bind oxygen. Low pH is acidic. High pH is basic. When CO2 is higher, pH is lower or acidic. When pH is acidic, hemoglobin is released to tissues that need oxygen. The relationship between oxygen affinity and pH Compare the biochemical structure of hemoglobin to myoglobin The molecular difference between normal and sickle forms of hemoglobin The difference between normal and sickle red blood cells at the cellular level How the diseased cells are different from normal red blood cells in their capacity to carry oxygen A normal RBC is round and concave shaped that easily moves through the bloodstream. A sickle hemoglobin releasing oxygen sticks together, forms fiber formations that causes the sickle appearance. This decreases the capacity to carry oxygen and also by not moving through smaller circulation easily causes blockages. Diagram explaining the molecular inheritance of sickle cell anemia References Hudon-Miller, S. (2012) Oxy vs Deoxy Hemoglobin. Retrieved from https:/ / www.youtube.com/watch?v=Tx4ZiJsFeAw Wolfe, G. (2000). Thinkwell Biochemistry. Retrieved from wgu.thinkwell.com. Hudon-Miller, S. (2012) Hemoglobin and myoglobin. Retrieved from http:/ /youtu.be/ qJyupSEVXlE

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