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

Hill Plot

Biochemistry

8. Protein Function

Hill Plot

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Multiple Choice

The slope of a Hill plot for hemoglobin _; whereas that for myoglobin __.

is about 3 in its cooperative state; is 1.0.

decreases at low pO₂ ; is constant at all pO₂.

increases at high pO₂ ; curves upward for all pO₂.

Is 1.0 ; is about 4.

Both A and B.

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Verified step by step guidance

Understand the Hill plot: A Hill plot is used to determine the cooperativity of ligand binding to a protein. The slope of the Hill plot, known as the Hill coefficient (n), indicates the degree of cooperativity.

Analyze hemoglobin's behavior: Hemoglobin exhibits cooperative binding, meaning its affinity for oxygen increases as more oxygen molecules are bound. In its cooperative state, the Hill coefficient for hemoglobin is typically around 3, indicating positive cooperativity.

Analyze myoglobin's behavior: Myoglobin, in contrast, binds oxygen non-cooperatively. It has a Hill coefficient of 1.0, indicating that its binding sites are independent and do not influence each other.

Consider the options: Option A states that the slope for hemoglobin is about 3 in its cooperative state, and for myoglobin, it is 1.0. This aligns with the known behavior of these proteins.

Consider option B: Option B states that the slope for hemoglobin decreases at low pO2, which is consistent with the fact that hemoglobin's cooperativity is less pronounced at low oxygen pressures. For myoglobin, the slope is constant at all pO2, which is true since it does not exhibit cooperativity.