Question 1. What is the O₂ saturation in the lungs? 2. What is the O₂ saturation in tissues at rest? 3. What percentage of O₂ is delivered to tissues at rest? 4. What is the O₂ saturation in exercising tissues? 5. What percentage of O₂ is delivered to exercising tissues? Cooperative binding Noncooperative 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
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The image presents an interactive table designed to compare cooperative binding and noncooperative binding in relation to oxygen (O₂) delivery. The objective is to illustrate why cooperative binding is an essential adaptation for efficient gas exchange. Below the table, there are draggable labels corresponding to various O₂ saturation levels, which can be applied to either binding type in answer to specific questions. 

**Table Structure:**

- **Columns:**
  - Cooperative Binding
  - Noncooperative Binding

- **Rows with Questions:**
  1. What is the O₂ saturation in the lungs?
  2. What is the O₂ saturation in tissues at rest?
  3. What percentage of O₂ is delivered to tissues at rest? (Highlighted in red)
  4. What is the O₂ saturation in exercising tissues?
  5. What percentage of O₂ is delivered to exercising tissues? (Highlighted in red)

**Draggable Labels for O₂ Saturation Levels:**
- 20%
- 30%
- 50%
- 70%
- 80%
- 100%

**Objectives:**
The goal is to drag and drop these saturation levels into the appropriate slots under each type of binding. Each saturation level is associated with a letter (e.g., a, b, c, etc.) for clarity and organization. Labels can be used multiple times.

This exercise emphasizes understanding the efficiency of cooperative binding over noncooperative binding in different physiological conditions, such as rest and exercise.
Transcribed Image Text:The image presents an interactive table designed to compare cooperative binding and noncooperative binding in relation to oxygen (O₂) delivery. The objective is to illustrate why cooperative binding is an essential adaptation for efficient gas exchange. Below the table, there are draggable labels corresponding to various O₂ saturation levels, which can be applied to either binding type in answer to specific questions. **Table Structure:** - **Columns:** - Cooperative Binding - Noncooperative Binding - **Rows with Questions:** 1. What is the O₂ saturation in the lungs? 2. What is the O₂ saturation in tissues at rest? 3. What percentage of O₂ is delivered to tissues at rest? (Highlighted in red) 4. What is the O₂ saturation in exercising tissues? 5. What percentage of O₂ is delivered to exercising tissues? (Highlighted in red) **Draggable Labels for O₂ Saturation Levels:** - 20% - 30% - 50% - 70% - 80% - 100% **Objectives:** The goal is to drag and drop these saturation levels into the appropriate slots under each type of binding. Each saturation level is associated with a letter (e.g., a, b, c, etc.) for clarity and organization. Labels can be used multiple times. This exercise emphasizes understanding the efficiency of cooperative binding over noncooperative binding in different physiological conditions, such as rest and exercise.
**Part C - Exploring the Cooperative Binding of Oxygen**

Oxygen shows cooperative binding to hemoglobin. Cooperative binding has the following effects on the binding and release of oxygen:

**Oxygen binding to hemoglobin:** When one molecule of oxygen binds to one of hemoglobin’s four subunits, the other subunits change shape slightly, increasing their affinity for oxygen.

**Oxygen release from hemoglobin:** When four oxygen molecules are bound to hemoglobin’s subunits and one subunit releases its oxygen, the other three subunits change shape again. This causes them to release their oxygen more readily.

These two graphs show how cooperative binding differs from a hypothetical situation where binding is not cooperative.

- The x-axis shows the partial pressure of oxygen (PO2). This is a measure of the amount of oxygen present in a tissue. The blue arrows on the x-axis show the partial pressure of oxygen in various tissues of the body.
- The y-axis shows the oxygen saturation of hemoglobin (O2 saturation). This is the percentage of oxygen-binding sites on hemoglobin molecules that are actually bound to oxygen.

**Graphs:**

1. **Cooperative Binding:**
   - The graph is a sigmoidal curve. As the PO2 increases, the O2 saturation of hemoglobin rises steeply before plateauing, indicating a sharp increase in binding efficiency once a certain threshold of oxygen is reached.

2. **Noncooperative Binding:**
   - The graph is a linear curve. As PO2 increases, O2 saturation of hemoglobin increases steadily at a constant rate, showing no enhanced binding efficiency as oxygen binds.

The table below walks you through a comparison of cooperative binding and noncooperative binding. By completing the table, you will learn why cooperative binding is an important adaptation that makes gas exchange more efficient.

*Drag the labels to their appropriate locations on the table. Labels can be used more than once.*
Transcribed Image Text:**Part C - Exploring the Cooperative Binding of Oxygen** Oxygen shows cooperative binding to hemoglobin. Cooperative binding has the following effects on the binding and release of oxygen: **Oxygen binding to hemoglobin:** When one molecule of oxygen binds to one of hemoglobin’s four subunits, the other subunits change shape slightly, increasing their affinity for oxygen. **Oxygen release from hemoglobin:** When four oxygen molecules are bound to hemoglobin’s subunits and one subunit releases its oxygen, the other three subunits change shape again. This causes them to release their oxygen more readily. These two graphs show how cooperative binding differs from a hypothetical situation where binding is not cooperative. - The x-axis shows the partial pressure of oxygen (PO2). This is a measure of the amount of oxygen present in a tissue. The blue arrows on the x-axis show the partial pressure of oxygen in various tissues of the body. - The y-axis shows the oxygen saturation of hemoglobin (O2 saturation). This is the percentage of oxygen-binding sites on hemoglobin molecules that are actually bound to oxygen. **Graphs:** 1. **Cooperative Binding:** - The graph is a sigmoidal curve. As the PO2 increases, the O2 saturation of hemoglobin rises steeply before plateauing, indicating a sharp increase in binding efficiency once a certain threshold of oxygen is reached. 2. **Noncooperative Binding:** - The graph is a linear curve. As PO2 increases, O2 saturation of hemoglobin increases steadily at a constant rate, showing no enhanced binding efficiency as oxygen binds. The table below walks you through a comparison of cooperative binding and noncooperative binding. By completing the table, you will learn why cooperative binding is an important adaptation that makes gas exchange more efficient. *Drag the labels to their appropriate locations on the table. Labels can be used more than once.*
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