Table of contents

1. A Review of General Chemistry5h 5m
2. Molecular Representations1h 14m
3. Acids and Bases2h 46m
4. Alkanes and Cycloalkanes4h 17m
5. Chirality3h 39m
6. Thermodynamics and Kinetics1h 22m
7. Substitution Reactions1h 48m
8. Elimination Reactions2h 30m
9. Alkenes and Alkynes2h 9m
10. Addition Reactions3h 19m
11. Radical Reactions1h 58m
12. Alcohols, Ethers, Epoxides and Thiols2h 40m
13. Alcohols and Carbonyl Compounds2h 17m
14. Synthetic Techniques1h 26m
15. Analytical Techniques:IR, NMR, Mass Spect7h 3m
16. Conjugated Systems6h 13m
17. Ultraviolet Spectroscopy51m
18. Aromaticity2h 34m
19. Reactions of Aromatics: EAS and Beyond5h 1m
20. Phenols55m
21. Aldehydes and Ketones: Nucleophilic Addition4h 56m
22. Carboxylic Acid Derivatives: NAS2h 51m
23. The Chemistry of Thioesters, Phophate Ester and Phosphate Anhydrides1h 10m
24. Enolate Chemistry: Reactions at the Alpha-Carbon1h 53m
25. Condensation Chemistry2h 9m
26. Amines1h 43m
27. Heterocycles2h 0m
28. Carbohydrates5h 53m
29. Amino Acids4h 20m
30. Peptides and Proteins2h 42m
31. Catalysis in Organic Reactions1h 30m
32. Lipids 2h 50m
33. The Organic Chemistry of Metabolic Pathways2h 52m
34. Nucleic Acids1h 32m
35. Transition Metals6h 14m
36. Synthetic Polymers1h 49m

3. Acids and Bases

Organic Chemistry Reactions

Organic Chemistry

3. Acids and Bases

Organic Chemistry Reactions

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Multiple Choice

Which of the following statements regarding competitive inhibitors is true?

Competitive inhibitors are permanently bound to the enzyme, leading to irreversible inhibition.

Competitive inhibitors increase the maximum reaction rate (Vmax) of an enzyme-catalyzed reaction.

Competitive inhibitors bind to the active site of an enzyme, preventing substrate binding.

Competitive inhibitors bind to an allosteric site, changing the enzyme's shape.

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Verified step by step guidance

Understand the role of competitive inhibitors in enzyme activity: Competitive inhibitors are molecules that bind to the active site of an enzyme, where the substrate normally binds.

Recognize the nature of competitive inhibition: Competitive inhibitors are not permanently bound to the enzyme. They can be displaced by an increase in substrate concentration, which is why the inhibition is reversible.

Analyze the effect on reaction kinetics: Competitive inhibitors do not change the maximum reaction rate (Vmax) of an enzyme-catalyzed reaction. Instead, they increase the apparent Km (Michaelis constant), indicating that a higher substrate concentration is needed to reach half of Vmax.

Differentiate between competitive and non-competitive inhibition: Unlike competitive inhibitors, non-competitive inhibitors bind to an allosteric site, not the active site, and can change the enzyme's shape, affecting Vmax.

Identify the correct statement: The correct statement is that competitive inhibitors bind to the active site of an enzyme, preventing substrate binding, which is a key characteristic of competitive inhibition.