The cooperative binding behavior of hemoglobin for oxygen is best explained by...
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The cooperative binding behavior of hemoglobin for oxygen is best explained by...
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- In an experiment, hemoglobin is dissociated in a buffer and a subunit is isolated to study for its oxygen binding affinity. (i) What is the shape of the oxygen dissociation curve is expected in the experiment?Explain why. (ii) Is the Km of the isolated subunit higher or lower than the Km of an intact hemoglobin?In oxygenated hemoglobin, pKa 5 6.6 forthe histidines at position 146 on the -chain. In deoxygenated hemoglobin, the pKa of these residues is 8.2. How can this piece ofinformation be correlated with the Bohr effect?A new oxygen transport protein that exhibits cooperative binding has been isolated and is beingstudied in the lab. Calculate the KD value if Y = 0.76 when pO2 = 18 torr (assume n = 2.5). Howdoes this compare to the KD value for hemoglobin? Does this protein bind more or less tightly tooxygen compared to hemoglobin?
- 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?A team of biochemists uses genetic engineering to modify the interface region between hemoglobin subunits. The resulting hemoglobin variants exist in solution primarily as αβ dimers (few, if any, α2β2 tetramers form). Are these variants likely to bind oxygen more weakly or more tightly? Explain your answer.To study the chemical properties of the blood hemoglobin of a vertebrate, it might seem convenient to remove the hemoglobin from the red blood cells so that hemoglobin is in simple aqueous solution. However, removing the hemoglobin from red blood cells often promptly alters its O2-binding characteristics. Explain why?
- The 2-3 phosphoglycerate (BFG) binds to the central gap formed by the hemoglobin monomers (a2b2) facilitating the reversible release of oxygen. Approximate relationships between BFG concentrations in red blood cells and Pos in hemoglobin are in the table.a) Draw the reaction schemeb) Write the forces that condition the union between hemoglobin and BFGA) illustrate in molecular detail how hemoglobin's reduced oxygen affinity is caused by protonation of the histidine side chain. b) what is the pKa of the histidine side-chain ionizable group expected to have?Apohemoglobin (apoHb) is a dimeric globular protein with two vacant heme‐binding. The preparationof apoHb is based on partial hemoglobin (Hb) unfolding to facilitate heme extraction into an organic solvent. What is an appropriate method for removing the heme? a. An acidic buffer to protonate the His axial ligand in the presence of ureaas the denaturing agent. b. An acidic buffer to protonate the His axial ligand in the presence of mercatoethanol as the denaturing agent. c. A basic buffer to deprotonate the His axial ligand in the presence of ureaas the denaturing agent. d. An basic buffer to protonate the His axial ligand in the presence of mercatoethanol as the denaturing agent.
- "Hemoglobin can be in either an oxy- or deoxy- state at a given pH. Given the appropriate pKa values, calculate fraction protonated at a given pH" How would I do this?) Dr Merrick is so excited to know the affinity constant Kd values for O2 binding to mammoth OBP and elephant hemoglobin at pH=7, that he starts speculating about the kinetics of binding to O2. If the ka value of mammoth EHb-O2 complex was the same as the ka value of mammoth OBP-O2 complex, what would be the ratio between the kd values of these complexes? Explain your reasoning. Hint: we are looking for the ratio kd(EHb)/kd(OBP) at pH=7.What qualitative effect would you expect each of the following to have onthe P50 of hemoglobin?(a) Increase in pH from 7.2 to 7.4(b) Increase in PCO2 from 20 to 40 mm Hg(c) Dissociation into monomer polypeptide chains(d) Decrease in 2,3-BPG concentration from 7 mM to 5 mM in red cells.