Chemistry Exam > Chemistry Videos > Inorganic Chemistry > Structure of Hemoglobin & Myoglobin
Structure of Hemoglobin & Myoglobin Video Lecture | Inorganic Chemistry
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FAQs on Structure of Hemoglobin & Myoglobin Video Lecture - Inorganic Chemistry
| 1. What is the primary function of hemoglobin and myoglobin? |  |
Ans. Hemoglobin is responsible for transporting oxygen from the lungs to tissues throughout the body, while myoglobin stores oxygen in muscle cells for use during periods of high activity.
| 2. How do the structures of hemoglobin and myoglobin differ? | |
Ans. Hemoglobin is a tetrameric protein composed of four subunits, each containing a heme group, while myoglobin is a monomeric protein with a single heme group.
| 3. How does the structure of hemoglobin allow for its role in oxygen transport? | |
Ans. The structure of hemoglobin includes a heme group in each subunit that can bind to oxygen, allowing for efficient oxygen transport through the bloodstream.
| 4. What is the significance of the iron atom in the heme group of hemoglobin and myoglobin? | |
Ans. The iron atom in the heme group is essential for binding and releasing oxygen molecules, facilitating the oxygen-carrying capacity of hemoglobin and myoglobin.
| 5. How do mutations in the genes coding for hemoglobin and myoglobin affect their structure and function? | |
Ans. Mutations in the genes coding for hemoglobin and myoglobin can lead to structural changes that impact their ability to bind oxygen, resulting in conditions such as sickle cell anemia or myoglobinuria.
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Nov 16, 2024 Last updated |
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