1. Proteins are also called polypeptides.
2. What are two examples of proteins? Enzymes, antibodies
3. What are the monomers of proteins? Amino acids
4. Draw the general structure of an amino acid: [Carboxyl group (-COOH), Amino group (-NH2), R group (side chain), Hydrogen atom, all bonded to a central carbon atom]
5. How many different amino acids are there? 20
6. Label the parts of the amino acid: [Central carbon, Carboxyl group, Amino group, R group, Hydrogen]
7. What is a peptide bond? A covalent bond formed between the carboxyl group of one amino acid and the amino group of another amino acid.
8. What is a dipeptide? Two amino acids joined by a peptide bond.
9. What is a polypeptide? A chain of many amino acids linked by peptide bonds.
10. What is the difference between a polypeptide and a protein? A polypeptide is a single chain of amino acids; a protein may consist of one or more polypeptides folded and coiled into a specific 3D shape.
11. What determines the shape of a protein? The sequence of amino acids (primary structure) and interactions between R groups.
12. What are the four levels of protein structure? Primary, secondary, tertiary, quaternary.
13. What is denaturation? The loss of a protein’s 3D structure due to disruption of non-covalent interactions, leading to loss of function.
14. What causes denaturation? Heat, pH changes, chemicals, heavy metals.
15. Can denatured proteins regain their function? Sometimes, if conditions return to normal and the primary structure is intact.
16. What are enzymes? Biological catalysts that speed up chemical reactions without being consumed.
17. What is the active site? The region of the enzyme where substrate binds and catalysis occurs.
18. What is the substrate? The molecule upon which an enzyme acts.
19. What is the induced fit model? The enzyme changes shape slightly when substrate binds to better fit the substrate.
20. What factors affect enzyme activity? Temperature, pH, substrate concentration, enzyme concentration, inhibitors.
21. What is an inhibitor? A molecule that decreases enzyme activity.
22. What is a competitive inhibitor? Binds to the active site, competing with substrate.
23. What is a non-competitive inhibitor? Binds to a site other than the active site, changing enzyme shape.
24. What is feedback inhibition? The end product of a metabolic pathway inhibits an enzyme early in the pathway.
25. What are cofactors? Non-protein molecules required for enzyme activity (e.g., metal ions).
26. What are coenzymes? Organic cofactors (e.g., vitamins).
27. What is the role of ATP in cellular processes? Provides energy for cellular work.
28. What is the structure of ATP? Adenine + ribose + three phosphate groups.
29. What happens during hydrolysis of ATP? ATP → ADP + Pi + energy.
30. What is the source of the Great Flood of Canada? Not a biology question; likely refers to geological/historical event unrelated to proteins/fungi.
Parent Tip: Review the logic above to help your child master the concept of protists worksheet.
