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

3. Amino Acids

Amino Acid Configuration

Biochemistry

3. Amino Acids

Amino Acid Configuration

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Multiple Choice

Which amino acid residues in hemoglobin are primarily carbamylated at low pH?

N-terminal amino groups of the globin chains

Side chains of aspartate residues

C-terminal carboxyl groups of the globin chains

Side chains of lysine residues

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Verified step by step guidance

Understand the concept of carbamylation: Carbamylation is a chemical reaction where a carbamoyl group (-CONH2) is added to amino groups. This process is influenced by pH, as low pH can protonate amino groups, making them less reactive.

Identify the functional groups in hemoglobin that can undergo carbamylation: Hemoglobin contains N-terminal amino groups, side chains of lysine residues, side chains of aspartate residues, and C-terminal carboxyl groups. Each of these groups has distinct chemical properties.

Analyze the reactivity of N-terminal amino groups: At low pH, the N-terminal amino groups are protonated, reducing their nucleophilicity and making them less likely to be carbamylated.

Evaluate the side chains of lysine residues: Lysine contains an ε-amino group in its side chain, which remains nucleophilic even at low pH, making it a primary target for carbamylation.

Consider the side chains of aspartate residues and C-terminal carboxyl groups: Both aspartate side chains and C-terminal carboxyl groups are negatively charged at physiological pH but become protonated at low pH, reducing their reactivity and likelihood of carbamylation.