**Text:**Given the graph below, what changes to % saturation of hemoglobin would you expect from the change in pH? *Increased* *Decreased***Diagram Explanation:**The graph titled "Effects of pH on Oxyhemoglobin Dissociation" depicts the relationship between the partial pressure of oxygen (P_O2 in mm Hg) on the x-axis and the percent saturation of hemoglobin on the y-axis. There are three curves, each representing a different pH level:- **pH 7.6**: The curve is shifted to the left, indicating a higher percent saturation of hemoglobin at a given P_O2. This suggests increased affinity of hemoglobin for oxygen at higher pH levels. - **pH 7.4**: This curve is in the middle and represents the standard physiological pH.- **pH 7.2**: The curve is shifted to the right, indicating a lower percent saturation of hemoglobin at a given P_O2. This suggests decreased affinity of hemoglobin for oxygen at lower pH levels.The graph illustrates how a decrease in pH (acidosis) leads to decreased hemoglobin saturation with oxygen at a given oxygen pressure, whereas an increase in pH (alkalosis) results in increased saturation. This represents the Bohr effect, where changes in pH affect hemoglobin’s binding affinity for oxygen. The image illustrates the chemical equilibrium involving carbon dioxide and water, represented by the following reaction:\[ \text{CO}_2 + \text{H}_2\text{O} \rightleftharpoons \text{H}_2\text{CO}_3 \rightleftharpoons \text{H}^+ + \text{HCO}_3^- \]**Explanation:**1. **Carbon Dioxide (CO₂) and Water (H₂O):** These reactants combine to form carbonic acid (H₂CO₃).2. **Carbonic Acid (H₂CO₃):** This intermediate compound can dissociate into hydrogen ions (H⁺) and bicarbonate ions (HCO₃⁻).3. **Equilibrium Arrows (⇌):** The double-headed arrows indicate that the reactions are reversible and can reach equilibrium.This process is significant in biological systems for maintaining pH balance and is a part of the carbonic acid-bicarbonate buffer system in blood.

Hemoglobin is a tetrameric protein, each subunit contains heme prosthetic group. One hemoglobin…

Answered: Given the graph below, what changes to…

Biochemistry

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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

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72.4.1
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?
At which temperature given does hemoglobin have a higher affinity for oxygen?
When a person develops a fever, which of the following statements hemoglobin saturation are correct? - Modify the structure of hemoglobin and decrease its affernity for O2 - Can shift the O2-hemoglobin dissociation curve to the right - Decrease O2 unloading occurs in the tissue - Modify the structure of hemoglobin and increase its affernity for O2 - Can shift the O2 hemoglobin dissociation curve to the left - Enhance O2 unloading occurs in the tissue
Which of the following is the concentration of hemoglobin-bound oxygen in the blood when the heme is fully saturated? 8500 uM 8630 uM 2200 uM 8800 uM
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…
Suppose you visit the Dalai Lama in Dharamsala, India (elevation 1460 m),and you begin to ponder the “big questions,” such as “What is the fractionalsaturation of the Dalai Lama’s hemoglobin?”(a) Assuming the Dalai Lama’s hemoglobin has a Hill coefficient = 3.2,and a P50 = 31 mm Hg, calculate the change in fractional O2 saturationof his hemoglobin going from his lungs (where PO2 = 85 mm Hg) to hiscapillaries (where PO2 = 25 mm Hg).(b) Why do you suppose the Dalai Lama’s hemoglobin has a P50 higher thannormal (where “normal” = 27 mm Hg)?
Which of the following is TRUE about carbon dioxide binding to hemoglobin? Carbon dioxide carbamoylates the N-terminus, stabilizing the T-state Carbon dioxide binds to the central cavity in hemoglobin, stabilizing the T-state. Carbon dioxide, binds to the heme iron, stabilizing the T-state. None of the above are true. 1 UNANSWERED QUESTION 1/1 SKIP FOR NOW 14:03 / 14:11 MacBook Pro
103) Emphysema is an obstructive type of disorder that results in a person having normal lung volumes but decreased forced expiratory reserve rates Group of answer choices True False 104) The Bohr Effect says that O2 is more easily released from hemoglobin as more H+ ions bind to the hemoglobin molecule. Group of answer choices True False 105) When you have very low levels of carbon dioxide in the blood due to hypocapnia or hyperventilation, the immediate affect is a decrease in the breathing rate Group of answer choices True False 106) Decreased blood pressure results in a decrease of the heart rate. Group of answer choices False True
Carbon monoxide (CO) is a colorless, odorless gas produced during combustion of fuels (for example, by car engines and furnaces). The following graph depicts an oxygen dissociation curve in the absence and presence of varying amounts of carbon monoxide. Based on these results, in the presence of 20% CO, when PO2 is 90mmHg you should expect each hemoglobin molecule to have _____ molecule(s) of O2 bound a) 1 b) 2 c) 3 d) 4

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Given the graph below, what changes to % saturation of hemoglobin would you expect from the change in pH? Decreased Increased Effects of pH on Oxyhemoglobin Dissociation Percent saturation of hemoglobin 100 80 60 40 20 0 pH 7.6 20 40 pH 7.4 pH 7.2 60 80 100