1. Draw an amino acid

2. Draw a dipeptide undergoing a hydrolysis reaction to for two amino acids

3. Draw two amino acids undergoing a dehydration reaction to form a dipeptide

4. Describe the primary structure of a polypeptide
Describe the primary structure of a polypeptide. (What type of bonds are formed, which parts of what type of molecules are involved?)

5. Describe the secondary structure of a protein
Describe the secondary structure of a protein. (What type of bonds are formed, which parts of what type of molecules are involved?)

6. Describe the tertiary structure of a protein
Describe the tertiary structure of a protein. (What type of bonds are formed, which parts of what type of molecules are involved?)

7. Describe the quarternary structure of a protein
Describe the quarternary structure of a protein. (What type of bonds are formed, which parts of what type of molecules are involved?)

8. What is meant by “form follows function”?

9. Name three examples of proteins and give their functions.

10. Distinguish between globular and fibrous proteins

11. Define the following terms: catalyst, activation energy, substrate, active site

12. Describe the effect of temperature on enzyme activity

13. Describe the effect of pH on enzyme activity

14. Describe the effect of substrate concentration on enzyme activity

15. What are immobilized enzymes and how they are used to produce lactose-free milk?

16. What is a metabolic pathway?

17. Describe how a non-competitive inhibitor affects enzyme activity.

18. Describe how a competitive inhibitor affects enzyme activity.

19. Compare and contrast coenzymes and cofactors.

20. Describe end product inhibition.