SANTA LAURENSIA SENIOR HIGH SCHOOL
CHEMISTRY CLASS | GRADE 11 | PROTEIN
Reading Comprehension Questions – Protein (Basic Level)
1. What is the monomer of a protein?
2. How many amino acids are essential and must be obtained from food?
3. What is the name of the polymer formed from amino acids?
4. What determines the sequence of amino acids in a protein?
5. What type of bond connects amino acids in a protein?
6. Which protein structure is described by the sequence of amino acids?
7. Name one function of proteins in the human body.
8. What type of interaction forms the secondary structure of proteins?
9. Give an example of a secondary protein structure.
10.What type of protein structure involves folding of the entire molecule?
11.What causes proteins to fold into a tertiary structure?
12.What happens to a protein during denaturation?
13.What kind of bond holds the tertiary structure of keratin together?
14.What is the difference between fibrous and globular proteins?
15.What is the name of the protein in red blood cells that carries oxygen?
16.How many polypeptide chains are there in hemoglobin?
17.What is the R group in an amino acid?
18.What is a zwitterion?
19.At which pH is leucine neutral?
20.What type of amino acid is hydrophilic—polar or nonpolar?
21.Which process joins amino acids together to form a peptide?
22.What is the result of the hydrolysis of a dipeptide?
23.What changes in pH can affect amino acid structure?
24.Which protein in the body contains a high percentage of cystine?
25.Why is heating egg white an example of irreversible denaturation?
📗 Intermediate Comprehension & Analysis Questions – Protein
1. Explain the role of the R group in determining the properties of an amino acid.
2. Why are proteins considered the most structurally and functionally diverse
macromolecules?
3. How does the primary structure affect the overall shape and function of a protein?
4. Describe how a single amino acid substitution can lead to a disorder such as sickle cell
anemia.
5. Compare and contrast alpha helices and beta-pleated sheets.
6. Explain how hydrogen bonds contribute to the secondary structure of proteins.
7. Identify and explain two types of interactions that stabilize the tertiary structure of
proteins.
8. Why are disulfide bridges important in protein structure?
9. Describe the significance of hydrophobic interactions in protein folding.
10.Explain how protein denaturation affects enzyme activity.
11.Discuss how pH can alter the ionic form of an amino acid like leucine.
12.Why is the quaternary structure only present in some proteins?
13.Compare fibrous and globular proteins in terms of structure and function.
14.Describe the sequence of structural changes from primary to quaternary in protein
formation.
15.How does protein structure relate to its function in enzymes?
16.Provide an example of a protein that has quaternary structure and describe its
components.
17.What is the relationship between amino acid polarity and protein solubility?
18.Explain how temperature can cause protein denaturation, using egg white as an
example.
19.Why are zwitterions important in amino acid chemistry?
20.Discuss the role of keratin and the significance of sulfur-containing amino acids in hair.
21.How does the body regulate protein synthesis to maintain function?
22.Describe the dehydration synthesis process in forming a peptide bond.
23.How is the sequence of amino acids in insulin related to its function in the human body?
24.Predict what would happen if polar amino acids were replaced by nonpolar ones in the
active site of an enzyme.
25.Explain how soap and detergent can disrupt protein structure.
