Some primitive animals have a hemoglobin that consists of two identical subunits. What would be the effect of this on the hemoglobin? It would have the same cooperativity as myoglobin. It would exhibit less cooperativity than hemoglobin. It would deliver more oxygen to the tissues than hemoglobin. It would have a hyperbolic binding curve. It would be less sensitive to the allosteric effectors such as 2,3- bisphosphoglycerate (BPG).
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- The graphs below show 02-binding curves of several proteins including myoglobin (Mb) and hemoglobin (Hb). If curve 3 (-) represents the 02 binding behavior of normal hemoglobin, which curve represents an 02-binding transporter with the same p50 as normal hemoglobin? 1.0- YO, 0.5 0.0 pO,(torr) O A. 1 B. 2 O C. 4 O D. 5 E. Both "2" and "4"Which of the following statements is false concerning the structure of hemoglobin? a. The binding of BPG stabilizes the T-state of Hb b. The R-state of Hb is favored under environments of high concentrations of O2 c. Hemoglobin's affinity for oxygen increases as protons ionize from the N-terminal tails d. Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons e. Hemoglobin favors the R-state in basic environmentsOne molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant).
- The O2-binding curve for Hemoglobin (Hb) is sigmoidal because: a O2 binding to Hb increases the binding affinity of Hb for additional O2. b The pH of blood is near the pKa of histidine. c The pH of the bloodstream changes with changes in O2 concentration. d Hb’s O2-binding affinity changes with changes in pH.There is an animal that uses almost 100 percent of the oxygen in its blood. Analyzing the Hb of this animal, it’s found that 2,3-BPG does not bind to Hb, but bicarbonate ions do. Knowing that bicarbonate ions are strong negative allosteric effectors, what do you make of these findings? Why is the animal’s Hb not responsive to 2,3 BGP, but responsive to bicarbonate ions?. In the experiments of Barrick, et al. ( observed that replacement of histidine by a noncovalently bonded imidazole not only reduced cooperativity but also increased the oxy- gen affinity of the hemoglobin. Suggest an explanation. it was
- The doctor also mentioned a new treatment for Sickle Cell Disease to JJ called Voxelotor (Oxbryta). Voxelotor binds to the a-globin chain and alters the structure of HbS stabilizing it in the R-state (relaxed state). Q7: In the presence of Voxelotor would you expect the affinity of HbS for O2 to increase or decrease? Q8: How would you classify the mechanism of action for Voxelotor?Does myoglobin exhibit a Bohr effect? Why or why not?he doctor also mentioned a new treatment for Sickle Cell Disease to JJ called Voxelotor (Oxbryta). Voxelotor binds to the a-globin chain and alters the structure of HbS stabilizing it in the R-state (relaxed state). Q7: In the presence of Voxelotor would you expect the affinity of HbS for O2 to increase or decrease? Q8: How would you classify the mechanism of action for Voxelotor? Q9: Voxelotor's structure is shown below. What would you expect the overall charge of the molecule to be in the blood (pH = 7.4) Pyridinium pKa = 2.6 Phenol pKa = 8.3
- You have discovered a new form of mouse myoglobin that has a p50 of 9 Torr. At approximately what pO2 would this hemoglobin be 86% saturated with oxygen? 85 Torr 40 Torr 60 Torr 55 Torr Not enough information is given to answer this questionSelect the hemoglobin variant(s) that are described by each statement. (a) The variant least likely to cause pathological symptoms. (b) The variant(s) likely to show pl values different from that of HbA on an isoelectric focusing gel. (c) The variant most likely to show a decrease in BPG binding and an increase in the overall affinity of the hemoglobin for oxygen. Answer Bank Hb Milwaukee Hb Cowtown Hb Memphis Hb Philly Hb Providence Hb Bibba HbSApproximate P50 for myoglobin from its binding curve. Approximate P50 for normal hemoglobin and the hemoglobin mutant from the binding curve. At low pO2 (below 20 Torr), which binds O2 with greater affinity, normal hemoglobin or the hemoglobin mutant? At high pO2 (above 30 Torr), which binds O2 with greater affinity, normal hemoglobin or the hemoglobin mutant? Which protein, normal hemoglobin or the hemoglobin mutant, transports O2 more efficiently? Briefly explain your answer.