(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…

(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)n Hb + nO₂ show 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 the table above including HbA where Ko2 represents the equi- librium dissociation constant for oxygen binding. If no curve is present for any of the mutant hemogobins, state the rea- son why the mutant is not represented. Indicate on the graph where its p50 would lie. PERCENT SATURATION 100- 80- 20- 0- 0 PARTIAL PRESSURE OF OXYGEN veins muscle lungs 20 40 60 80 OXYGEN PRESSURE (millimeters of mercury) 100 120 T 140

(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)n Hb + nO₂ show 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 the table above including HbA where Ko2 represents the equi- librium dissociation constant for oxygen binding. If no curve is present for any of the mutant hemogobins, state the rea- son why the mutant is not represented. Indicate on the graph where its p50 would lie. PERCENT SATURATION 100- 80- 20- 0- 0 PARTIAL PRESSURE OF OXYGEN veins muscle lungs 20 40 60 80 OXYGEN PRESSURE (millimeters of mercury) 100 120 T 140

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Explain why the gas values from the alveolar air to the blood change during pulmonary gas exchange. For example: Alveolar air for CO2 has a value of 40mmHg then when entering the blood shifts to 45mmHg. Why does this occur? I tried to calculate this by using Dalton’s law but I’m not Understanding.
Will a decrease in carbon dioxide (CO2) shift the binding curve of hemoglobin? Will it shift to the left or right?
Below are multiple oxygen binding affinity curves for hemoglobin. The affinity curve for normal hemoglobin in blood is represented by curve "D," at a pH of 7.2 and at a concentration of 5mM BPG and 26 mM CO2. O₂ saturation (%) 100 Answer 1: B Answer 2: [Select] Answer 3: B Answer 4: 80 A 60 1. How would changes to acidity, BPG concentration and CO₂ levels affect the binding affinity curve and p50? lower than Answer 5: E 40 1. BPG concentration is decreased to 3mM: The binding affinity curve would look like B. The p50 would be lower than normal (D). 2. pH is increased to 7.6: The binding affinity curve would look like B. The p50 would be [Select] normal (D). 20 3. CO₂ concentration is increased to 30 mM: The binding affinity curve would look like. [Select] The p50 would be Answer 6: 0 normal (D). II. The hemoglobin has been treated with a denaturing solution which disrupts quaternary structure only, and has a binding affinity resembling myoglobin. The binding affinity curve would look…
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