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 Groups

Biochemistry

3. Amino Acids

Amino Acid Groups

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Multiple Choice

In the catalytic mechanism of lysozyme, what is the state of Glutamic acid 35 (Glu35) and Aspartic acid 52 (Asp52) at the end of the reaction?

Glu35 is protonated and Asp52 is deprotonated.

Both Glu35 and Asp52 are protonated.

Glu35 is deprotonated and Asp52 is protonated.

Both Glu35 and Asp52 are deprotonated.

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Verified step by step guidance

Understand the catalytic mechanism of lysozyme: Lysozyme is an enzyme that cleaves the glycosidic bond in bacterial cell walls. The active site contains two key residues, Glutamic acid 35 (Glu35) and Aspartic acid 52 (Asp52), which play critical roles in the reaction.

Analyze the roles of Glu35 and Asp52 during the reaction: Glu35 acts as a proton donor, facilitating the cleavage of the glycosidic bond, while Asp52 stabilizes the transition state by forming a covalent intermediate with the substrate.

Consider the state of Glu35 at the end of the reaction: After donating its proton, Glu35 becomes deprotonated, as it has released its proton to assist in the catalytic process.

Examine the state of Asp52 at the end of the reaction: Asp52 forms a covalent bond with the substrate during the reaction, and at the end of the process, it regains a proton, becoming protonated.

Conclude the states of Glu35 and Asp52: At the end of the reaction, Glu35 is deprotonated, and Asp52 is protonated, reflecting their roles in the catalytic mechanism of lysozyme.