Myoglobin and Hemoglobin Paul Rosevear, PhD 10/3/13

Objectives: Concerning myoglobin and hemoglobin

1. Define the physiological roles of myoglobin and hemoglobin. 2. Specify the molecular architecture of an oxygen binding protein; what would be the specific function of the heme and why is it essential to have it bound and surrounded by globin? 3. Can a case be made for stating that the entire protein matrix of both myoglobin and hemoglobin is necessary to insure the proper oxidation and ligand status of iron? 4. Contrast the molecular consequences of oxygen binding to myoglobin and hemoglobin; how do these properties relate to physiological function? 5. Explain the role of CO2, pH, BPG and subunit interactions with respect to oxygen binding in hemoglobin. 6. Explain the molecular events occurring upon O2 binding to the -subunit of Hb. 7. Evaluate the consequences of amino acid mutations in hemoglobin especially with respect to those occurring in the interior region near the heme group as opposed to the solvent accessible surface.
Concerning Sickle Cell Disease and Other Pathologies

1. Explain the nature of the specific mutation giving rise to sickle cell anemia and what molecular changes are generated in terms of secondary, tertiary or quaternary structure. 2. Contrast the red blood cell morphologies of individuals containing hemoglobin S and hemoglobin A, respectively. What is the influence of pH and oxygen tension in these cells? 3. Explain the connection between the chemical-physical properties of Hemoglobin S and the onset of anemia and other clinical features.