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 statements about the oxygen-hemoglobin interaction is true?

The oxygen dissociation curve for hemoglobin is hyperbolic.

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

Hemoglobin binds oxygen with equal affinity at all four subunits, regardless of how many O$_2$ molecules are already bound.

Oxygen binding to hemoglobin is a non-cooperative process.

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Verified step by step guidance

Step 1: Understand the concept of oxygen-hemoglobin interaction. Hemoglobin is a tetrameric protein that binds oxygen in a cooperative manner, meaning the binding of one oxygen molecule affects the affinity of the remaining binding sites for oxygen.

Step 2: Review the oxygen dissociation curve for hemoglobin. The curve is sigmoidal (S-shaped), not hyperbolic, which reflects the cooperative binding of oxygen. This is due to the conformational changes in hemoglobin upon oxygen binding.

Step 3: Analyze the statement about affinity. Binding of one O$_2$ molecule to hemoglobin increases the affinity for additional O$_2$ molecules. This is known as positive cooperativity and is a key feature of hemoglobin's function.

Step 4: Evaluate the statement about equal affinity. Hemoglobin does not bind oxygen with equal affinity at all four subunits. The affinity changes as oxygen binds, due to conformational shifts between the T (tense) and R (relaxed) states of hemoglobin.

Step 5: Consider the statement about cooperativity. Oxygen binding to hemoglobin is a cooperative process, not a non-cooperative one. This cooperative behavior is essential for efficient oxygen transport and release in tissues.