The graph below shows the O₂-binding curves for myoglobin (Mb) and hemoglobin(Hb).a.10080604020002040 60 80 100pO₂ (torr)a. Use the graph to determine the Kd of myoglobin for O₂ (show your approach).Write that in the provided space.b. What is the difference between myoglobin and hemoglobin that cause the O₂-binding curves to so be different? Answer in the provided space.c. Why is it important that hemoglobin has these particular O₂-bindingcharacteristics? Answer in the provided space.YO₂

Introduction: Oxygen binding is the binding of an oxygen molecule to a specific functional protein…

Answered: The graph below shows the O₂-binding…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Identify the human form of hemoglobin that is produced most abundantly in the adult.A. two -globin chains (alpha) and two -globin chains (beta)B. two -globin chains (beta) and two -globin chains (gamma)C. two -globin chains (gamma) and two -globin chains (delta)D. two -globin chains (delta) and two -globin chains (epsilon)E. two -globin chains (epsilon) and two -globin chains (zeta)
Which of the following statements does NOT apply to the K value in the equation for the oxygen binding curve of myoglobin? It is numerically equal to p50. O A. It is defined as that oxygen partial pressure at which half of the oxygen binding sites are occupied. В. If Y> K, then myoglobin is less than 50% saturated with oxygen. OC. O D. It is a measure of the affinity of myoglobin for oxygen. OE. It is the value of po2 at which Y = 0.5.
Following several days at high altitude the body responds to the decreased oxygen content of the atmosphere by increasing the amount of 2,3-bisphosphoglycerate it produces. Based on this information and refering to the graph below, identify the correct response from the options. Y (fraction saturation) 1.0 0.8 0.6 0.4 0.2 0.0 0 20 Oxygen Binding plot 40 60 p02 (torr) 80 100 A) Curve y=high altitude and gives a greater release of oxygen to the tissues B) Curve x = high altitude and gives a greater release of oxygen to the tissues C) Curve y=high altitude and allows more oxygen to be bound at low oxygen levels D) Curve x = high altitude and allows more oxygen to be bound at low levels
Below is the O₂ binding curve for adult Hb in whole blood (containing BPG) shown in red (labelled Hb). Fraction of Hb bound with Oxygen 1.0 0.8 0.6 0.4 0.2 0.0 0 20 40 pO2 (torr) 60 80 ABC c. Which curve lacks cooperativity? [Select] Hb 100 a. Which curve is the best representation for stripped Hb (pure hemoglobin with heme, but no other small allosteric molecules associated)? [Select] b. Which curve has the lowest affinity (as measured by the p50)? [Select]
72.4.1
Which is/are false? a. Carbaminohemoglobin is hemoglobin bound to carbon dioxide b. In the lungs, the oxyhemoglobin saturation curve undergoes a 'left shift' c. At a PO2 of 10 mmHg, there is more deoxyhemoglobin in blood that oxyhemoglobin d. Higher temperatures and lower pH cause hemoglobin to bind more readily with oxygen than in conditions of lower temperatures and higher pH
Individuals with cystic fibrosis produce thick mucus in the lungs, resulting in a higher-than-normal level of CO2 in the blood. What is the problem that results from higher-than-normal levels of COz in the blood? Please relate this to buffers in the blood and construct a clear problem statement.
Suppose a hypothetical "molecule X" binds to hemoglobin (at a different site than the O2 binding site) and stabilizes the T state. How would you identify this effector? a. Positive homotropic effector b. Negative homotropic effector c. Positive heterotropic effector d. Negative heterotropic effector
Below are multiple oxygen binding affinity curves for hemoglobin. The affinity curve for normal hemoglobin in blood is represented by curve "D," at a pH of 7.2 and at a concentration of 5mM BPG and 26 mM CO2. O₂ saturation (%) 100 Answer 1: B Answer 2: [Select] Answer 3: B Answer 4: 80 A 60 1. How would changes to acidity, BPG concentration and CO₂ levels affect the binding affinity curve and p50? lower than Answer 5: E 40 1. BPG concentration is decreased to 3mM: The binding affinity curve would look like B. The p50 would be lower than normal (D). 2. pH is increased to 7.6: The binding affinity curve would look like B. The p50 would be [Select] normal (D). 20 3. CO₂ concentration is increased to 30 mM: The binding affinity curve would look like. [Select] The p50 would be Answer 6: 0 normal (D). II. The hemoglobin has been treated with a denaturing solution which disrupts quaternary structure only, and has a binding affinity resembling myoglobin. The binding affinity curve would look…
Why is the decreased affinity of fetal hemoglobin for BPG advantageous? With fewer BPG molecules bound to heme, there are more heme residues available for O2 binding. O A. B. Decreased BPG binding biases the fetal hemoglobin toward the R state. C. More free BPG is available to bind to adult hemoglobin, resulting in a shift to the R state. BPG is more available to bind to fetal myoglobin. helping to release O2 in fetal muscle tissue. D. 47
There is an animal that uses almost 100 percent of the oxygen in its blood. Analyzing the Hb of this animal, it’s found that 2,3-BPG does not bind to Hb, but bicarbonate ions do. Knowing that bicarbonate ions are strong negative allosteric effectors, what do you make of these findings? Why is the animal’s Hb not responsive to 2,3 BGP, but responsive to bicarbonate ions?
In the absence of 2,3-bisphosphoglycerate, the binding of oxygen by hemoglobin: a. is characterized by cooperativity b. resembles that of myoglobin c. binds at the end of the hemoglobin molecule d. is stabilized as the deoxy conformation of hemoglobin for the release into capillaries

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