Q21 With regards to hemoglobin-oxygen binding, CO₂ is a [Select]modulator and 2,3-bisphosphoglycerate is a [Select]With regards to hemoglobin-oxygen binding, CO2 is a ✓ [Select]positvenegativemodulator and 2,3-bisphosphoglycerate is a[SelecWith regards to hemoglobin-oxygen binding, CO₂ is amodulator and 2,3-bisphosphoglycerate is a ✔ [ Select ]positivenegative[Select]allostericallosteric modulator.Vallostericric modulator.allostericallosteric modulator.

Positive allosteric modulators of haemoglobin -oxygen binding are the agents that stabilise R state…

Answered: With regards to hemoglobin-oxygen…

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 3SQE

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Describe how the following allosteric effectors regulated Hemoglobin’s O2 affinity: • CO2• H+ (pH; Explain the basis for the Bohr Effect)• 2,3-BPG • CO
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?
(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…
Will a mutation from Distal histidine to phenylalanine shift the binding curve of hemoglobin?Will it shift the curve to the left or right, shift to myoglobin or no longer bind to O2?
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 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
Describe the structural basis for the cooperative (allosteric) binding of O2 by hemoglobin but not by myoglobin
Help me please
This graph shows the O2 binding curves of Hemoglobin. Which one is the R-state curve, and which one is the T-state? Why these curves are different comparing to the normal curve (middle one) 1.0 0.8 Observed hemoglobin- binding curve 0.6 0.4 0.2 0.0 50 100 150 200 p02 (torr) Y (fractional saturation)
Name three effects produced by H+ binding to hemoglobin.
How does the concentration of 2,3 BPG affect hemoglobin's P50 for oxygen? select the correct answer A) BPG binds to the N-terminus of Hemoglobin's alpha 2 subunit and increase hemoglobin's P50 for oxygen. B) BPG binds to the heme blocking oxygen's ability to bind and lowering hemoglobin's P 50. C) As the BPG increases hemoglobin's P50 for oxygen increase. D) As the BPG increases hemoglobin's P50 for oxygen decreases. E) BPG does not affect hemoglobin's P50 for oxygen
a) How much more O2 can be transported by the blood when erythrocytesleave the lungs? Consider that a normal adult has a concentration of 15 g hemoglobin/100 mL of bloodand that the hemoglobin is 98% saturated with O2 at the usual pO2 of 100 torr in the lung at sea level. b) On the basis of the graph, explain how myoglobin facilitates the diffusion of O2 through muscle cells. Would myoglobin be effective as an O2-transport protein in cells of other tissues? Explain.

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