Chem 210 Biochemistry Final Exam Preparation Newest
With Complete 100 Questions And Correct Detailed
Answers| Brand New Version!
Chem 210 Biochemistry Final Exam Preparation
Questions 1–200
Biomolecules & Structure (1–10)
Q1. Which functional group is characteristic of amino acids?
A) Hydroxyl
B) Amino and carboxyl
C) Carbonyl
D) Phosphate
A1: B — Amino acids contain both an amino (-NH₂) and a carboxyl (-COOH) group.
Q2. Scenario: A researcher isolates a molecule containing four fused rings and hydroxyl groups. What
biomolecule is this likely to be?
A) Carbohydrate
B) Lipid (steroid)
C) Protein
D) Nucleic acid
A2: B — Steroids are lipids with four fused rings; hydroxyl groups indicate potential for hydrogen
bonding.
Q3. Which of the following is a common monosaccharide?
A) Glucose
B) Sucrose
C) Lactose
D) Maltose
A3: A — Glucose is a monosaccharide; sucrose, lactose, and maltose are disaccharides.
,Q4. Scenario: A polypeptide has a sequence rich in cysteine residues. Which structure is most influenced
by cysteine?
A) Primary
B) Secondary
C) Tertiary
D) Quaternary
A4: C — Cysteine residues form disulfide bonds, stabilizing tertiary structure.
Q5. Which type of bond stabilizes alpha-helices and beta-sheets in proteins?
A) Disulfide
B) Hydrogen
C) Ionic
D) Covalent
A5: B — Hydrogen bonds stabilize secondary structures like alpha-helices and beta-sheets.
Q6. Scenario: A nucleic acid sample is digested with DNase. Which component will remain intact?
A) DNA backbone
B) RNA molecules
C) Phosphate groups
D) Deoxyribose
A6: B — DNase specifically cleaves DNA; RNA is unaffected.
Q7. Which lipid class forms biological membranes?
A) Triacylglycerols
B) Phospholipids
C) Steroids
D) Waxes
A7: B — Phospholipids form the bilayer structure of cell membranes.
Q8. Scenario: A protein loses function when a hydrogen bond between backbone amides is disrupted.
Which structure is affected?
A) Primary
B) Secondary
C) Tertiary
D) Quaternary
A8: B — Hydrogen bonds between backbone amides stabilize secondary structure.
Q9. Which nucleotide is used exclusively in RNA?
A) Thymidine
B) Uridine
C) Cytidine
D) Guanosine
A9: B — Uridine (U) is found only in RNA; DNA uses thymidine (T).
,Q10. Scenario: A peptide chain folds due to hydrophobic interactions in the interior. Which level of
structure is primarily involved?
A) Primary
B) Secondary
C) Tertiary
D) Quaternary
A10: C — Tertiary structure is stabilized by hydrophobic interactions among side chains.
Enzyme Function & Kinetics (11–20)
Q11. Which is a coenzyme derived from vitamin B3?
A) FAD
B) NAD⁺
C) CoA
D) Biotin
A11: B — NAD⁺ is derived from niacin (vitamin B3).
Q12. Scenario: An enzyme’s Vmax remains unchanged, but Km increases after inhibitor addition. Type of
inhibition?
A) Competitive
B) Noncompetitive
C) Uncompetitive
D) Mixed
A12: A — Competitive inhibitors increase Km without affecting Vmax.
Q13. Which amino acid side chain is most likely to act as a general acid in enzyme catalysis?
A) Alanine
B) Histidine
C) Glycine
D) Valine
A13: B — Histidine can donate or accept protons at physiological pH.
Q14. Scenario: An allosteric enzyme displays a sigmoidal velocity vs. substrate curve. Which is true?
A) Follows Michaelis-Menten kinetics
B) Cooperative binding occurs
C) Inhibition is irreversible
D) Enzyme is saturated at low substrate
A14: B — Sigmoidal kinetics indicate cooperative substrate binding.
Q15. Which type of inhibition decreases both Vmax and Km?
A) Competitive
B) Noncompetitive
, C) Uncompetitive
D) Mixed
A15: C — Uncompetitive inhibitors bind only to the enzyme-substrate complex, lowering both Vmax and
Km.
Q16. Scenario: A mutation in the enzyme’s active site reduces binding affinity. Likely effect on Km?
A) Decrease
B) Increase
C) No change
D) Cannot determine
A16: B — Reduced affinity increases Km.
Q17. Which cofactor is required for pyruvate dehydrogenase activity?
A) NAD⁺
B) FAD
C) CoA
D) All of the above
A17: D — Pyruvate dehydrogenase requires NAD⁺, FAD, and CoA.
Q18. Scenario: A kinase transfers a phosphate group from ATP to a substrate. Which type of enzyme?
A) Oxidoreductase
B) Transferase
C) Hydrolase
D) Ligase
A18: B — Kinases are transferases; they transfer functional groups.
Q19. Which enzyme mechanism forms a transient covalent intermediate with the substrate?
A) Michaelis-Menten
B) Covalent catalysis
C) Allosteric regulation
D) Competitive inhibition
A19: B — Covalent catalysis involves transient covalent bonding between enzyme and substrate.
Q20. Scenario: An enzyme has Km = 2 mM and Vmax = 100 μmol/min. Substrate = 2 mM. Velocity?
A) 25 μmol/min
B) 50 μmol/min
C) 100 μmol/min
D) 75 μmol/min
A20: B — Using Michaelis-Menten: V = (Vmax × [S]) / (Km + [S]) = (100 × 2)/(2+2) = 50 μmol/min.
Metabolism & Bioenergetics (21–30)
With Complete 100 Questions And Correct Detailed
Answers| Brand New Version!
Chem 210 Biochemistry Final Exam Preparation
Questions 1–200
Biomolecules & Structure (1–10)
Q1. Which functional group is characteristic of amino acids?
A) Hydroxyl
B) Amino and carboxyl
C) Carbonyl
D) Phosphate
A1: B — Amino acids contain both an amino (-NH₂) and a carboxyl (-COOH) group.
Q2. Scenario: A researcher isolates a molecule containing four fused rings and hydroxyl groups. What
biomolecule is this likely to be?
A) Carbohydrate
B) Lipid (steroid)
C) Protein
D) Nucleic acid
A2: B — Steroids are lipids with four fused rings; hydroxyl groups indicate potential for hydrogen
bonding.
Q3. Which of the following is a common monosaccharide?
A) Glucose
B) Sucrose
C) Lactose
D) Maltose
A3: A — Glucose is a monosaccharide; sucrose, lactose, and maltose are disaccharides.
,Q4. Scenario: A polypeptide has a sequence rich in cysteine residues. Which structure is most influenced
by cysteine?
A) Primary
B) Secondary
C) Tertiary
D) Quaternary
A4: C — Cysteine residues form disulfide bonds, stabilizing tertiary structure.
Q5. Which type of bond stabilizes alpha-helices and beta-sheets in proteins?
A) Disulfide
B) Hydrogen
C) Ionic
D) Covalent
A5: B — Hydrogen bonds stabilize secondary structures like alpha-helices and beta-sheets.
Q6. Scenario: A nucleic acid sample is digested with DNase. Which component will remain intact?
A) DNA backbone
B) RNA molecules
C) Phosphate groups
D) Deoxyribose
A6: B — DNase specifically cleaves DNA; RNA is unaffected.
Q7. Which lipid class forms biological membranes?
A) Triacylglycerols
B) Phospholipids
C) Steroids
D) Waxes
A7: B — Phospholipids form the bilayer structure of cell membranes.
Q8. Scenario: A protein loses function when a hydrogen bond between backbone amides is disrupted.
Which structure is affected?
A) Primary
B) Secondary
C) Tertiary
D) Quaternary
A8: B — Hydrogen bonds between backbone amides stabilize secondary structure.
Q9. Which nucleotide is used exclusively in RNA?
A) Thymidine
B) Uridine
C) Cytidine
D) Guanosine
A9: B — Uridine (U) is found only in RNA; DNA uses thymidine (T).
,Q10. Scenario: A peptide chain folds due to hydrophobic interactions in the interior. Which level of
structure is primarily involved?
A) Primary
B) Secondary
C) Tertiary
D) Quaternary
A10: C — Tertiary structure is stabilized by hydrophobic interactions among side chains.
Enzyme Function & Kinetics (11–20)
Q11. Which is a coenzyme derived from vitamin B3?
A) FAD
B) NAD⁺
C) CoA
D) Biotin
A11: B — NAD⁺ is derived from niacin (vitamin B3).
Q12. Scenario: An enzyme’s Vmax remains unchanged, but Km increases after inhibitor addition. Type of
inhibition?
A) Competitive
B) Noncompetitive
C) Uncompetitive
D) Mixed
A12: A — Competitive inhibitors increase Km without affecting Vmax.
Q13. Which amino acid side chain is most likely to act as a general acid in enzyme catalysis?
A) Alanine
B) Histidine
C) Glycine
D) Valine
A13: B — Histidine can donate or accept protons at physiological pH.
Q14. Scenario: An allosteric enzyme displays a sigmoidal velocity vs. substrate curve. Which is true?
A) Follows Michaelis-Menten kinetics
B) Cooperative binding occurs
C) Inhibition is irreversible
D) Enzyme is saturated at low substrate
A14: B — Sigmoidal kinetics indicate cooperative substrate binding.
Q15. Which type of inhibition decreases both Vmax and Km?
A) Competitive
B) Noncompetitive
, C) Uncompetitive
D) Mixed
A15: C — Uncompetitive inhibitors bind only to the enzyme-substrate complex, lowering both Vmax and
Km.
Q16. Scenario: A mutation in the enzyme’s active site reduces binding affinity. Likely effect on Km?
A) Decrease
B) Increase
C) No change
D) Cannot determine
A16: B — Reduced affinity increases Km.
Q17. Which cofactor is required for pyruvate dehydrogenase activity?
A) NAD⁺
B) FAD
C) CoA
D) All of the above
A17: D — Pyruvate dehydrogenase requires NAD⁺, FAD, and CoA.
Q18. Scenario: A kinase transfers a phosphate group from ATP to a substrate. Which type of enzyme?
A) Oxidoreductase
B) Transferase
C) Hydrolase
D) Ligase
A18: B — Kinases are transferases; they transfer functional groups.
Q19. Which enzyme mechanism forms a transient covalent intermediate with the substrate?
A) Michaelis-Menten
B) Covalent catalysis
C) Allosteric regulation
D) Competitive inhibition
A19: B — Covalent catalysis involves transient covalent bonding between enzyme and substrate.
Q20. Scenario: An enzyme has Km = 2 mM and Vmax = 100 μmol/min. Substrate = 2 mM. Velocity?
A) 25 μmol/min
B) 50 μmol/min
C) 100 μmol/min
D) 75 μmol/min
A20: B — Using Michaelis-Menten: V = (Vmax × [S]) / (Km + [S]) = (100 × 2)/(2+2) = 50 μmol/min.
Metabolism & Bioenergetics (21–30)
