(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

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Chapter1: The Human Body: An Orientation
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(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-
60-
40-
20-
PARTIAL PRESSURE OF OXYGEN
lungs
veins muscle
0-
0 20
bc/d
T
100 120 140
40 60 80
OXYGEN PRESSURE
(millimeters of mercury)
(c)
Of the mutant hemoglobins in the table above, which form a hydrogen bond stabilizing the
R (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 the
allosteric 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 table
above according to the expected value of Lo.
(e) For the mutant hemoglobins in the table above, will the mutation sites likely cause structural
distortions affecting the binding of 2,3-bisphosphoglycerate (BPG)? Explain.
Transcribed Image Text:(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- 60- 40- 20- PARTIAL PRESSURE OF OXYGEN lungs veins muscle 0- 0 20 bc/d T 100 120 140 40 60 80 OXYGEN PRESSURE (millimeters of mercury) (c) Of the mutant hemoglobins in the table above, which form a hydrogen bond stabilizing the R (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 the allosteric 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 table above according to the expected value of Lo. (e) For the mutant hemoglobins in the table above, will the mutation sites likely cause structural distortions affecting the binding of 2,3-bisphosphoglycerate (BPG)? Explain.
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