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

Hydrogen ions bind to the ______ portion of a hemoglobin molecule.

oxygen-binding site

globin (protein)

heme (iron)

porphyrin ring

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Verified step by step guidance

Understand the structure of hemoglobin: Hemoglobin is a protein composed of four subunits, each containing a heme group and a globin protein. The heme group includes an iron atom bound within a porphyrin ring.

Recognize the role of hydrogen ions in hemoglobin function: Hydrogen ions (H⁺) influence hemoglobin's ability to bind and release oxygen, a process known as the Bohr effect.

Identify the binding site for hydrogen ions: Hydrogen ions bind to specific amino acid residues in the globin portion of hemoglobin, altering its conformation and oxygen-binding affinity.

Differentiate between the components: The heme group is responsible for oxygen binding via the iron atom, while the globin protein interacts with hydrogen ions to regulate hemoglobin's function.

Conclude that hydrogen ions bind to the globin (protein) portion of hemoglobin, not the heme (iron) or porphyrin ring, as these are involved in oxygen binding rather than pH regulation.