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 Carbonation & Protonation

Biochemistry

8. Protein Function

Hemoglobin Carbonation & Protonation

Previous problemNext problem

Struggling with Biochemistry?

Join thousands of students who trust us to help them ace their exams!Watch the first video

Multiple Choice

Choose all of the following molecules that, when bound, trigger hemoglobin's transition from T to R state.

CO₂

O₂

2,3-Bisphosphoglycerate

H⁺

Previous problemNext problem

Verified step by step guidance

Understand the T (tense) and R (relaxed) states of hemoglobin: Hemoglobin can exist in two main conformations, the T state, which has a lower affinity for oxygen, and the R state, which has a higher affinity for oxygen.

Identify the role of oxygen (O2) in hemoglobin's transition: Oxygen binding to hemoglobin stabilizes the R state, facilitating the transition from the T state to the R state.

Consider the effect of other molecules: CO2, H+, and 2,3-Bisphosphoglycerate (2,3-BPG) are known to stabilize the T state, thus promoting oxygen release rather than binding.

Recognize the role of carbon monoxide (CO): CO binds to hemoglobin with a high affinity, but it does not trigger the T to R transition; instead, it prevents oxygen from binding effectively.

Conclude that O2 is the molecule that, when bound, triggers the transition from the T state to the R state in hemoglobin, enhancing its oxygen-binding capacity.