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…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter46: Gas Exchange: The Respiratory System

Section: Chapter Questions

Problem 9TYK

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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?
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?
What is the molecular basis for the difference in the electrophorentic pattern between normal hemoglobin A and hemoglobin S?
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.
Is the cooperative binding of oxygen by hemoglobin better described by the concerted or the sequential model?
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
Increasing concentrations of either 2,3-bisphosphoglycerate (BPG) or protons (H +) cause a ____________ ( rightward OR leftward) shift of the hemoglobin/oxygen binding curve. However, the mechanisms by which these two substances mediate this effect are distinct. Compare & contrast the way by which BPG and protons interact with hemoglobin and thereby influence its structure and function
Referring to the loading and unloading of oxygen from hemoglobin (as illustrated in the figure), which of the following statements is correct? Oxygen Dissociation Curve.png Group of answer choices When a person in ventilating at rest, 75% of hemoglobin is still oxyhemoglobin The percent saturation of hemoglobin is higher at higher partial pressures of oxygen A decrease in the pH of the blood would promote unloading oxygen from the hemoglobin All of these are correct
Which hemoglobin has a higher affinity for O2 at the tissue pO2 of around 4 kPa?
Which of the following concerning hemoglobin is true? a) BPG decreases at high altitudes and causes more O2 offloading in tissues b) As pH increases, [CO2] increases in tissues, causing more O2 release in tissue c) The R state is stabilized by CO2 binding, whereas the T state is stabilized by O2 binding d) About 38% of oxygen dissociates from hemoglobin in tissues e) Hemoglobin has a higher affinity for oxygen than carbon monoxide My guess is D.
Which of the following concerning hemoglobin is true? a) BPG decreases at high altitudes and causes more O2 offloading in tissues b) As pH increases, [CO2] increases in tissues, causing more O2 release in tissue c) The R state is stabilized by CO2 binding, whereas the T state is stabilized by O2 binding d) About 38% of oxygen dissociates from hemoglobin in tissues e) Hemoglobin has a higher affinity for oxygen than carbon monoxide My guess is D. What following statement is TRUE concerning motifs and domains? a) Both motifs and domains are independently stable. b) Domains undergo dynamic individual changes that affect the entire protein c) B-a-ß loops, B barrels, and helix-turn-helix structure are types of domains d) Motifs and domains are part of secondary structural elements e) Ab initio computations predict motif folds accurately a majority of the time My guess is B. Which of the following is TRUE under the following conditions: an enzyme displaying Michaelis-Menten kinetics…
does BPG bind to deoxyhemoglobin only？why BPG does not bind to oxyhemoglobin？ what is chemical structure difference between deoxyhemoglobin and oxyhemoglobin？

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