TY - CHAP M1 - Book, Section TI - Proteins: Myoglobin & Hemoglobin A1 - Kennelly, Peter J. A1 - Rodwell, Victor W. A2 - Rodwell, Victor W. A2 - Bender, David A. A2 - Botham, Kathleen M. A2 - Kennelly, Peter J. A2 - Weil, P. Anthony PY - 2018 T2 - Harper's Illustrated Biochemistry, 31e AB - OBJECTIVESAfter studying this chapter, you should be able to:Describe the most important structural similarities and differences between myoglobin and hemoglobin.Sketch binding curves for the oxygenation of myoglobin and hemoglobin.Identify the covalent linkages and other close associations between heme and globin in oxymyoglobin and oxyhemoglobin.Explain why the physiologic function of hemoglobin requires a sigmoidal rather than hyperbolic O2-binding curve.Explain the role of the distal histidine on the ability of hemoglobin to bind carbon monoxide (CO).Define P50 and indicate its significance in oxygen transport and delivery.Describe the structural and conformational changes in hemoglobin that accompany its oxygenation and subsequent deoxygenation.Explain the role of 2,3-bisphosphoglycerate (BPG) in oxygen binding and delivery.Explain how the Bohr effect enhances the ability of red blood cells to transport CO2 and deliver it to the lungs.Describe the structural consequences to hemoglobin S (HbS) of lowering Po2.Identify the metabolic defect that occurs as a consequence of α and β thalassemias. SN - PB - McGraw-Hill Education CY - New York, NY Y2 - 2024/03/29 UR - accesspharmacy.mhmedical.com/content.aspx?aid=1160188876 ER -