7. Draw a diagram of the heme complexes in deoxyhemoglobin and oxyhemoglobin (complete porphyrin structures are not required, but show all iron coordination positions).
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- 1. The diagram on the right compares the O₂ binding prop- erties of normal adult hemoglobin (HbA) to those of one dubbed Hb Great-Lakes characterized by the mutation Leu(368) His. In the dia- gram Y = fraction of heme groups with bound O₂, and pO2, the par- tial pressure of O2 above the solution, is measured in units of torr or mmHg. Draw the corresponding Hill plot, being careful to reproduce graph- ically the dissociation equilibrium constant for O₂ binding (Ko2) for y each hemoglobin and to show the difference in the extent of allo- stery or cooperativity of subunit interaction in each type of hemo- globin. You need draw only the central, linear portion of the Hill plot. State what is the likely magnitude of the Hill constant (nH) for HbA from your reading and state what is the likely range of the magni- tude of the Hill coefficient for Hb Great Lakes. 1.0 0.8 0.6 0.4 0.2 Hb Great Lakes 0 10 20 Hb A 1 1 30 40 pO₂ (torr) I 50 601. The diagram on the right compares the O2 binding prop- 1.0 r erties of normal adult hemoglobin (HbA) to those of one dubbed Hb Great-Lakes characterized by the mutation Leu(B68)His. In the dia- gram Y= fraction of heme groups with bound O2, and pO2, the par- tial pressure of O2 above the solution, is measured in units of torr or mmHg. Hb Great Lakes 0.8 Hb A 0.6 Draw the corresponding Hill plot, being careful to reproduce graph- ically the dissociation equilibrium constant for O2 binding (Ko2) for Y each hemoglobin and to show the difference in the extent of allo- stery or cooperativity of subunit interaction in each type of hemo- globin. 0.4 You need draw only the central, linear portion of the Hill plot. 0.2 State what is the likely magnitude of the Hill constant (nH) for HbA from your reading and state what is the likely range of the magni- tude of the Hill coefficient for Hb Great Lakes. 0 10 20 30 40 50 60 pO2 (torr)Which of the following are true of normal adult hemoglobin? Choice 1 of 4:can bind four Fe2+ ions Choice 2 of 4:can covalently bind four O2 molecules Choice 3 of 4:can adopt 2 different conformations, with different orientations of αβ dimers Choice 4 of 4:can bind four BPG molecules to stabilize the T state
- 2.HbF is the predominant hemoglobin of embrions.It has two γ-and two α-subunits(α2γ2).HbF does not bind 2,3-BPG well.What is the affinity of oxygen binding for HbF in compare with HbA?For answer: 1)Explain the function of HbA and the role of 2,3-BPG in the regulation of O2 binding. 2)Draw the oxygen-binding curves of HbA and HbF. 3)Mark the Biology significance of the difference in O2 affinity for HbA and HbF.28. What is the function of the proximal histidine in hemoglobin? MARK ALL THAT APPLY. Group of answer choices Prevents the oxidation of the iron in the heme prosthetic group Converts oxygen into carbon dioxide. Coordinates the iron in the heme prosthetic group. Prevents formation of superoxide ion. Stabilizes the bound oxygen through direct coordination.3. When muscles are more active physiological conditions change to affect oxygen binding to Hemoglobin. Briefly describe the changes that occur and why this affects hemoglobin function. Draw the shifted curve on the graph above. A. What physiological conditions change during exercise (levels of what molecules are increasing/decreasing)? B. How do these molecules directly affect Hb’s structure ? What interactions does this stabilize ? C. How do these interactions affect the affinity of Hb for O2? How would this affect the binding curve for Hb? Draw on the graph provided. D. How will this shift in the binding curve affect the function of Hemoglobin ? E.Where does the physiological pO2 in the tissues fall on the O2 binding curve ? In the lungs ? Why is this physiologically important?
- Which of the following statements about the I state of hemoglobin is FALSE? a, iron ion is pulled to the plane of the heme ring b. stabilized by ion pairing at the dimers interface c. 2,3-bisphosphoglycerate shifts the RT equilibrium towards the T state O d. tense state of hemoglobinWhich of the following is incorrect about 2,3-bisphosphoglycerate (BPG)? It is highly (-) charged b. It prevents binding of O₂ to hemoglobin Oc. It binds only to the relaxed (oxy) conformation of hemoglobin Od. It binds in the space between the four subunits of hemoglobin a.1. What is the role of carbonic anhydrase in red blood cells at the tissue site? 2. Write the correct term that correlates with each the following symbols Hb = HbO2 = HbCO2 H+ O2 H2CO3 HHb HCO3 3. Using the symbols above and any others you may need, draw an illustration that shows the flow of O2 from lungs to tissue and CO2 from tissue to lungs.
- 8. Factor affecting the affinity of hemoglobin for oxygen a. Briefly describe how the following 4 factors affect the affinity of hemoglobin for oxygen: i. Bohr effect - ii. Carbon dioxide - iii. Temperature - iv. 2,3-bisphosphoglycerate - b. Fetal hemoglobin has affinity for O2 compared to adult hemoglobin.12. Explain how the oxygen dissociation curve is related to the properties and function of hemoglobin.Hemoglobin and myoglobin both use heme as their prosthetic group and they both bind O2. However, their O2-binding curves indicate these proteins have different activities. What lind of information can be learned about the differences between the curves?