Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

8. Protein Function

Hemoglobin Cooperativity

Biochemistry

8. Protein Function

Hemoglobin Cooperativity

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Multiple Choice

Which of the following is an example of cooperativity in hemoglobin?

The hydrolysis of ATP by hemoglobin to release energy.

The irreversible denaturation of hemoglobin at high temperatures.

Hemoglobin binding to carbon dioxide at the N-terminal amino groups.

The binding of one O$_2$ molecule to hemoglobin increases the affinity for additional O$_2$ molecules.

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Verified step by step guidance

Understand the concept of cooperativity: Cooperativity refers to a phenomenon where the binding of a molecule to a protein affects the binding affinity of subsequent molecules. In hemoglobin, this is observed in oxygen binding.

Recall the structure of hemoglobin: Hemoglobin is a tetrameric protein composed of four subunits, each capable of binding one oxygen (O$_2$) molecule. The subunits interact with each other, which is key to cooperativity.

Explain the mechanism of oxygen binding: When the first O$_2$ molecule binds to one subunit of hemoglobin, it induces a conformational change in the protein structure. This change increases the affinity of the remaining subunits for O$_2$, making it easier for additional O$_2$ molecules to bind.

Relate this to the correct answer: The binding of one O$_2$ molecule to hemoglobin increasing the affinity for additional O$_2$ molecules is a classic example of positive cooperativity. This is distinct from other processes like ATP hydrolysis or carbon dioxide binding, which do not involve cooperative interactions.

Conclude the explanation: Cooperativity in hemoglobin is essential for efficient oxygen transport in the body, as it allows hemoglobin to load oxygen in the lungs and release it in tissues where oxygen is needed.