pO2 intissuesp02 inlungs1.00Oxygen-bindingcurves for normalNormal Hbhemoglobin, 50%carboxyhemoglobin,and hemoglobin from0.8an anemic individual.0.6Y50% COHB0.4-Anemic individual0.24812pO2 (kPa)Box 5-1 Figure 2Lehninger Principles of Biochemistry, Seventh EditionO 2017 W. H. Freeman and Companyr aye i UIEI. Answer the following questions. Do not forget the units.1) From the binding curve for normal Hb shown above, what is the Ka of normal hemoglobin?

The oxygen-dissociation curve shows the affinity of oxygen with the hemoglobin protein. The process…

Answered: pO2 in tissues p02 in lungs 1.00…

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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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 variant of hemoglobin (Boston variant; mutation His E7(58)α → Tyr) promotes methemoglobin formation involving the α (alpha) subunits. What is the maximum value of the Hill constant (n) that you could measure for the Boston variant of hemoglobin? log (YO2 / 1 - YO2 ) = log pO2 - logP50 Please break down each step of the Hill equation and explain why the result for n is valid from a logical standpoint.
30. The cooperative binding behavior of hemoglobin for oxygen is best explained by... Group of answer choices The movement of the proximal histidine upon O2 binding causes a structural change at the binding interface between subunits The oxidation of Fe2+ to Fe3+ and formation of the superoxide ion causes distortion of the protoporphyrin ring, altering binding interface between subunits The tetrameric nature of hemoglobin's quaternary structure directly confers cooperative binding activity The movement of the distal histidine upon O2 binding causes a structural change at the binding interface between subunits The binding of O2 causes a pH shift that changes the protonation state of amino acids located at the interface between subunits The solubility of hemoglobin in aqueous solution and its insolubility in nonpolar environments
A person was found to have very low levels of functional beta globin mRNA and therefore very low levels of the beta globin protein. What problems would this cause for assembling functional haemoglobin molecules?
In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to the Hill coefficient
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?
Approximate nH for each protein from its Hill plot. Which proteins exhibits a greater degree of positive cooperativity, normal hemoglobin or the mutant hemoglobin?
In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to the Hillcoefficient? Explain your answers.
In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to (A)oxygen affinity, (B)the Bohr effect, and (C)the Hillcoefficient? Explain your answers.
You have discovered a new hemoglobin variant you are calling Hb-21. You have noticed the following from your studies of Hb-21: - The binding constant of Hb-21 is the same at pH 7.1 and 7.4.- The binding constant curves generated by Hb-21 and O2 are sigmoidal.- The Hill coefficient for Hb-21 is 3.-The binding constant for Hb-21 with O2 in the presence of 5mM 2,3-bisphosphglycerate is about 6-times lower instead of the 8-times lower that is observed under these conditions for the wild type enzyme. Use this information to answer questions: Based on this information which of these features of hemoglobin would you conclude are altered in Hb-21 as compared to the wild type hemoglobin? ____ the cooperativity.____ the amount of T versus R state in the tissues. ____ the Bohr effect. What is the major issue for an individual with the Hb-21 variant? Explain exactly what aspect of hemoglobin’s function is altered.
An antibody binds to another protein with anequilibrium constant, K, of 5 × 109 M–1. When it binds toa second, related protein, it forms three fewer hydrogenbonds, reducing its binding affinity by 11.9 kJ/mole. Whatis the K for its binding to the second protein? (Free-energychange is related to the equilibrium constant by the equa-tion ΔG° = –2.3 RT log K, where R is 8.3 × 10–3 kJ/(mole K)and T is 310 K.)
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

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