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3. Explain why the structure of myoglobin makes it function well as an oxygen-storage protein whereas the structure of hemoglobin makes it function well as an oxygen-transport protein. Discuss this in terms of the binding curve below and include the role of cooperativity in your answer. Percent O₂ saturation 100 80 60 40 20 0 0 Working muscle 20 Resting muscle Myoglobin Hemoglobin Venous po₂ 40 60 80 Partial pressure of oxygen (po, torr) Arterial po₂ 100 120 4. What is the effect of pH on the binding of oxygen to hemoglobin (the Bohr Effect)? What happens to the percent saturation as a function of pO₂ graph as a result of pH change (include graph)? Why is there a pH difference in tissues versus the lungs? Briefly describe how the Bohr Effect contributes to oxygen transport to the tissues. 5. How does BPG binding to hemoglobin decrease its affinity for oxygen?

3. Explain why the structure of myoglobin makes it function well as an oxygen-storage protein whereas the structure of hemoglobin makes it function well as an oxygen-transport protein. Discuss this in terms of the binding curve below and include the role of cooperativity in your answer. Percent O₂ saturation 100 80 60 40 20 0 0 Working muscle 20 Resting muscle Myoglobin Hemoglobin Venous po₂ 40 60 80 Partial pressure of oxygen (po, torr) Arterial po₂ 100 120 4. What is the effect of pH on the binding of oxygen to hemoglobin (the Bohr Effect)? What happens to the percent saturation as a function of pO₂ graph as a result of pH change (include graph)? Why is there a pH difference in tissues versus the lungs? Briefly describe how the Bohr Effect contributes to oxygen transport to the tissues. 5. How does BPG binding to hemoglobin decrease its affinity for oxygen?

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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3. Explain why the structure of myoglobin makes it function well as an oxygen-storage protein whereas the structure of hemoglobin makes it function well as an oxygen-transport protein. Discuss this in terms of the binding curve below and include the role of cooperativity in your answer. 100 80 Percent O₂ saturation 8 60 20 Working muscle 20 Resting muscle Myoglobin Hemoglobin Venous po₂ 60 40 80 Partial pressure of oxygen (pO₂, torr) Arterial po 100 120 4. What is the effect of pH on the binding of oxygen to hemoglobin (the Bohr Effect)? What happens to the percent saturation as a function of po2 graph as a result of pH change (include graph)? Why is there a pH difference in tissues versus the lungs? Briefly describe how the Bohr Effect contributes to oxygen transport to the tissues. 5. How does BPG binding to hemoglobin decrease its affinity for oxygen?
Transcribed Image Text:3. Explain why the structure of myoglobin makes it function well as an oxygen-storage protein whereas the structure of hemoglobin makes it function well as an oxygen-transport protein. Discuss this in terms of the binding curve below and include the role of cooperativity in your answer. 100 80 Percent O₂ saturation 8 60 20 Working muscle 20 Resting muscle Myoglobin Hemoglobin Venous po₂ 60 40 80 Partial pressure of oxygen (pO₂, torr) Arterial po 100 120 4. What is the effect of pH on the binding of oxygen to hemoglobin (the Bohr Effect)? What happens to the percent saturation as a function of po2 graph as a result of pH change (include graph)? Why is there a pH difference in tissues versus the lungs? Briefly describe how the Bohr Effect contributes to oxygen transport to the tissues. 5. How does BPG binding to hemoglobin decrease its affinity for oxygen?
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