Give detailed Solution with explanation (no need Handwritten The binding of oxygen by hemoglobin is modulated by 2,3-bisphosphoglycerate (2,3-BPG). Indicate which of the following statements apply to this modulation.(Select all that apply.)Positive charges in the interior of hemoglobin form salt bridges with the negative charges on 2,3-BPG.The half-saturation Po, value for hemoglobin is dramatically increased when 2,3-BPG is present.The carboxy terminal nitrogens of the two a subunits of hemoglobin interact with the negative charges on 2,3-BPG.The half-saturation Po, value for hemoglobin is dramatically decreased when 2,3-BPG is present.

Introduction 2,3-BPG (2,3-bisphosphoglycerate) is a small molecule that is involved in regulating…

Answered: The binding of oxygen by hemoglobin is…

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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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?
The 2-3 phosphoglycerate (BFG) binds to the central gap formed by the hemoglobin monomers (a2b2) facilitating the reversible release of oxygen. Approximate relationships between BFG concentrations in red blood cells and Pos in hemoglobin are in the table.a) Draw the reaction schemeb) Write the forces that condition the union between hemoglobin and BFG
Oxygen has an allosteric interaction with hemoglobin. What are the results of this interaction as oxygen a) binds to and b) is released from hemoglobin?
What effect does hyperventilation have on blood pH and why? What simple measure can be used to correct the pH imbalance and how does it work? What effect would hyperventilation have on hemoglobin O2 saturation in a normal healthy individual? What effect would a PaO2 of 60 mmHg have on hemoglobin O2 saturation and why? (explain in terms of the O2-Hb dissociation curve)
After spending a day or more at high altitude (with an oxygen partial pressure of 75 torr), the concentration of 2,3- bisphosphoglycerate (2,3-BPG) in red blood cells increases. What effect would an increased concentration of 2,3-BPG have on the oxygen-binding curve for hemoglobin? Why would this adaptation be beneficial for functioning well at high altitude?
The hemoglobin of a human fetus differs from adult hemoglobin. Compare the dissociation curves of the two hemoglobins in the graph at right. Describe how they differ, and propose a hypothesis to explain the benefit of this difference.
What is the role of 2, 3-Bisphosphoglycerate (2,3-BPG) in the function of haemoglobin as an oxygen carrier molecule? Explain the binding mechanism and effect of 2,3-BPG leading to the reduced oxygen binding affinity for haemoglobin and transitions in the T (deoxygenated) and R (oxygenated) states of haemoglobin.
Which of the following statements is false concerning the structure of hemoglobin? a. The binding of BPG stabilizes the T-state of Hb b. The R-state of Hb is favored under environments of high concentrations of O2 c. Hemoglobin's affinity for oxygen increases as protons ionize from the N-terminal tails d. Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons e. Hemoglobin favors the R-state in basic environments
Studies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain astructural variant of hemoglobin, HbF, consisting of two α and two γ subunits (α2 γ2 ), whereas maternal erythrocytes contain HbA (α2β2).(a) Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF? Explain.(b) What is the physiological significance of the different O2 affinities?(c) When all the BPG is carefully removed from samples of HbA and HbF, the measured O2 -saturation curves (and consequently the O2 affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O2 -saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O2 affinity of hemoglobin? How can the above information be used to explain the different O2 affinities of fetal and…
Studies of oxygen transport in pregnant mammals have shown that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two γ and two β subunits (γ2β2), whereas maternal erythrocytes contain HbA (α2β2). (a) Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF? Explain. (b) What is the physiological significance of the different O2 affinities? (c) When all the BPG is carefully removed from samples of HbA and HbF, the measured O2-saturation curves (and consequently the O2 affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O2-saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O2 affinity of hemoglobin? How can the above information be used to explain the different O2 affinities of…
Explain how the binding of molecular oxygen (O2) to haemoglobin affects the tertiary structures of each monomer. Hence, explain how this influences the quaternary structure of the haemoglobin molecule, and how this helps haemoglobin to transport O2 from the lungs to the muscles.
The primary allosteric regulator of hemoglobin oxygen affinity is ( ) and functions by stabilizing the ( ) state of enzyme.

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