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

The binding of Oxygen to stabilize the R-state of Hemoglobin is best explained by which model(s)?

Concerted Model.

Sequential Model.

Neither.

Combination of Both.

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Verified step by step guidance

Understand the two models: The Concerted Model (also known as the Monod-Wyman-Changeux model) suggests that all subunits of a protein are in the same state (either all R or all T), and the binding of a ligand shifts the equilibrium towards the R state. The Sequential Model (also known as the Koshland-Némethy-Filmer model) proposes that subunits change state individually upon ligand binding, leading to a mix of T and R states.

Recognize that Hemoglobin is a tetrameric protein with four subunits, each capable of binding oxygen. The binding of oxygen to one subunit can influence the state of the other subunits.

Consider the physiological role of Hemoglobin: It must efficiently pick up oxygen in the lungs (high oxygen concentration) and release it in tissues (low oxygen concentration). This requires a cooperative binding mechanism.

Analyze how the combination of both models explains Hemoglobin's behavior: The Concerted Model accounts for the overall shift from T to R state as more oxygen binds, while the Sequential Model explains the intermediate states and the gradual increase in oxygen affinity.

Conclude that the combination of both models provides a comprehensive explanation for the cooperative binding of oxygen to Hemoglobin, as it incorporates both the global conformational changes and the stepwise binding process.