Q13: **Educational Website Transcription: Hemoglobin and Myoglobin Binding Curves**### Graph ExplanationThe graph visualizes the binding curves of adult hemoglobin (in green) and myoglobin (in red) at pH 7.4, incorporating 2,3-bisphosphoglycerate. The hemoglobin binding curve is sigmoidal due to its four interacting oxygen-bound sites, while the myoglobin curve is hyperbolic, representing its single oxygen-bound site.### Binding Curve ShiftsDetermine whether the hemoglobin binding curve will shift left or right under the following scenarios:#### Shifts Left1. **Hemoglobin is isolated from red blood cells and stripped of 2,3-bisphosphoglycerate.**2. **Tetrameric hemoglobin is dissociated into its subunits.**3. **The adult hemoglobin (HbA) is replaced by an infant's fetal hemoglobin (HbF).**#### Shifts Right1. **The concentration of 2,3-bisphosphoglycerate increases during acclimation to high altitude.**2. **The CO₂ concentration in the blood increases.**3. **The blood pH drops from 7.4 to 7.2.**### Graph Details- **X-axis**: Partial pressure of oxygen (pO₂) in torr.- **Y-axis**: Fraction of binding sites occupied.The myoglobin curve remains relatively flat and quickly saturates as pO₂ increases, whereas the hemoglobin curve starts with a low fraction of occupied sites and increases sharply, indicating cooperative binding.

The oxygen dissociation curve of hemoglobin is a crucial concept in understanding how…

The The graph represents the adult hemoglobin binding curve (in green) at pH 7.4 in the presence of 2,3-bisphosphoglycerate. hemoglobin binding curve has a sigmoidal shape, due to four interacting oxygen-bound sites. For comparison, the myglobin binding curve has only one oxygen-bound site and has a hyperbolic curve. For each of the six scenarios, determine whether the hemoglobin binding curve would shift left or shift right. Shifts left Answer Bank Hemoglobin is isolated from red blood cells and stripped of 2,3-bisphosphoglycerate. Tetrameric hemoglobin is dissociated into its subunits. The concentration of 2,3-bisphosphoglycerate increases during acclimation to high altitude. Fraction of binding sites occupied The adult hemoglobin (HbA) is replaced by an infant's fetal hemoglobin (HbF). 0.9 0.8 0.7 0.6 0.5 0.4 0.3 0.2 0.1 0.0 0 20 Myoglobin 40 The CO₂ concentration in the blood increases. Hemoglobin 60 po₂ (torr) Shifts right 80 The blood pH drops from 7.4 to 7.2. 100 12

The The graph represents the adult hemoglobin binding curve (in green) at pH 7.4 in the presence of 2,3-bisphosphoglycerate. hemoglobin binding curve has a sigmoidal shape, due to four interacting oxygen-bound sites. For comparison, the myglobin binding curve has only one oxygen-bound site and has a hyperbolic curve. For each of the six scenarios, determine whether the hemoglobin binding curve would shift left or shift right. Shifts left Answer Bank Hemoglobin is isolated from red blood cells and stripped of 2,3-bisphosphoglycerate. Tetrameric hemoglobin is dissociated into its subunits. The concentration of 2,3-bisphosphoglycerate increases during acclimation to high altitude. Fraction of binding sites occupied The adult hemoglobin (HbA) is replaced by an infant's fetal hemoglobin (HbF). 0.9 0.8 0.7 0.6 0.5 0.4 0.3 0.2 0.1 0.0 0 20 Myoglobin 40 The CO₂ concentration in the blood increases. Hemoglobin 60 po₂ (torr) Shifts right 80 The blood pH drops from 7.4 to 7.2. 100 12

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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Q13:

**Educational Website Transcription: Hemoglobin and Myoglobin Binding Curves**

### Graph Explanation
The graph visualizes the binding curves of adult hemoglobin (in green) and myoglobin (in red) at pH 7.4, incorporating 2,3-bisphosphoglycerate. The hemoglobin binding curve is sigmoidal due to its four interacting oxygen-bound sites, while the myoglobin curve is hyperbolic, representing its single oxygen-bound site.

### Binding Curve Shifts
Determine whether the hemoglobin binding curve will shift left or right under the following scenarios:

#### Shifts Left

1. **Hemoglobin is isolated from red blood cells and stripped of 2,3-bisphosphoglycerate.**
2. **Tetrameric hemoglobin is dissociated into its subunits.**
3. **The adult hemoglobin (HbA) is replaced by an infant's fetal hemoglobin (HbF).**

#### Shifts Right

1. **The concentration of 2,3-bisphosphoglycerate increases during acclimation to high altitude.**
2. **The CO₂ concentration in the blood increases.**
3. **The blood pH drops from 7.4 to 7.2.**

### Graph Details
- **X-axis**: Partial pressure of oxygen (pO₂) in torr.
- **Y-axis**: Fraction of binding sites occupied.

The myoglobin curve remains relatively flat and quickly saturates as pO₂ increases, whereas the hemoglobin curve starts with a low fraction of occupied sites and increases sharply, indicating cooperative binding.

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Step 1: Factors Influencing the Hemoglobin Oxygen Dissociation Curve

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