(b)The diagram on the right compares O2-dissoci-ation curves for human hemoglobins characterized by dif-ferent p50 values. If Ko2 represents the equilibrium disso-ciation constant for oxygen binding, e.g.,Hb(02)nHb + nO₂show the relationship between Ko2 and p50.Assign one of the curves (a, b, e) that best approxi-mates the Ko2 of each of the mutant hemoglobins in thetable above including HbA where Ko2 represents the equi-librium dissociation constant for oxygen binding. If no curveis present for any of the mutant hemogobins, state the rea-son why the mutant is not represented. Indicate on thegraph where its p50 would lie.PERCENT SATURATION100-80-60-40-20-PARTIAL PRESSURE OF OXYGENlungsveins muscle0-0 20bc/dT100 120 14040 60 80OXYGEN PRESSURE(millimeters of mercury)(c)Of the mutant hemoglobins in the table above, which form a hydrogen bond stabilizing theR (oxy) conformation similarly to that in wild type HbA. Justify this statement on the basis of the pa-rameters characterizing the mutant hemoglobin.(d)According to the MWC model of hemoglobin function, the equilibrium constant for theallosteric transition between the two quaternary structures in the absence of ligand is defined as:Lo= [To] / [Ro]where the subscript indicates no subunit is occupied by ligand. Rank the hemoglobins in the tableabove according to the expected value of Lo.(e) For the mutant hemoglobins in the table above, will the mutation sites likely cause structuraldistortions affecting the binding of 2,3-bisphosphoglycerate (BPG)? Explain.

These curves depict the binding of oxygen to hemoglobin, and the various mutants of hemoglobin may…

Answered: (b) The diagram on the right compares…

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

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Below is the equation that represents O2 binding to hemoglobin. Hb+4O2⇌Hb(O2)According to Le Chatelier’s principle, which form of the hemoglobin (Hb or Hb(O2)4) is predominant in the lungs where the partial pressure of oxygen is high? Explain. I need help answering this
Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated α subunit binds oxygen, but the O2 -saturation curve ishyperbolic rather than sigmoid. In addition, the binding of oxygen to the isolated α subunit is not affected by the presence of H+, CO2 , or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?
Below is a fractional saturation curve for O₂ binding to adult hemoglobin. Assume that curve Y represents a condition at pH 7.4 and with a normal physiological level of 2,3-BPG. Curve X represents a condition that Fractional saturation (0) 0.2 0.0 0 Tissue PO, (kPa) 12 Lungs
Under appropriate denaturing conditions, hemoglobin can dissociate into four separate subunits. An isolated alpha subunit binds oxygen, but the O2-saturation curve is hyperbolic rather than sigmoid. In addition, the binding of oxygen to an isolated alpha subunit is not affected by the presence of H+, CO2, or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?
In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.
Below is the O₂ binding curve for adult Hb in whole blood (containing BPG) shown in red (labelled Hb). Fraction of Hb bound with Oxygen 1.0 0.8 0.6 0.4 0.2 0.0 0 20 40 pO2 (torr) 60 80 ABC c. Which curve lacks cooperativity? [Select] Hb 100 a. Which curve is the best representation for stripped Hb (pure hemoglobin with heme, but no other small allosteric molecules associated)? [Select] b. Which curve has the lowest affinity (as measured by the p50)? [Select]
Suppose you visit the Dalai Lama in Dharamsala, India (elevation 1460 m),and you begin to ponder the “big questions,” such as “What is the fractionalsaturation of the Dalai Lama’s hemoglobin?”(a) Assuming the Dalai Lama’s hemoglobin has a Hill coefficient = 3.2,and a P50 = 31 mm Hg, calculate the change in fractional O2 saturationof his hemoglobin going from his lungs (where PO2 = 85 mm Hg) to hiscapillaries (where PO2 = 25 mm Hg).(b) Why do you suppose the Dalai Lama’s hemoglobin has a P50 higher thannormal (where “normal” = 27 mm Hg)?
Name 3 conditions (ex: pO2) in which the oxygen dissociation curve will shift to the left. Additionally, when there is such a shift to the left, does that mean that hemoglobin's affinity for O2 has increased or decreased?
The O2-binding curves for normal haemoglobin (Hb A) and a mutant haemoglobin (Hb Kempsey) are shown in the diagram. Which of the following statements, based on this graph, are true? 1.0 0.8 Hb/Kempsey 0.6 Hb A 0.4 0.2 0.0 20 40 60 80 100 p02 (torr) 1. Hb Kempsey has a higher affinity for O, than HbA 2. Hb Kempsey is unable to transition between the R and T states 3. Hb Kempsey demonstrates cooperative binding of oxygen. 4. Hb Kempsey's curve could be explained by a loss of nearly all the cooperative interactions between the subunits. 5. A possible explanation for the curve observed with Hb Kempsey is mutation at His HC3. 2,4,5. O 1.2,5. O 1,2,3,4,5. O 2,3,4. O 1.2.4. Y (Fraction Saturation)
From your graph, estimate the P50 for normal hemoglobin and the mutant corresponding to your student number and explain if these results support your expectations regarding the mutant's oxygen affinity compared to normal hemoglobin. ف C Normal Yakima pO2 (torr) Yo2 Yo2 10 0.05 0.10 15 0.10 0.25 20 0.25 0.45 25 0.50 0.70 30 0.75 0.85 40 0.85 0.95 60 0.95 0.98 H
Which hemoglobin has a higher affinity for O2 at the tissue pO2 of around 4 kPa?
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