CHEM 210 FINAL EXAM STUDY GUIDE 2026 –
COMPLETE CONCEPT REVIEW & PRACTICE
MATERIALS (LATEST EDITION)
Biochemistry 210: Final Exam Practice Questions
Section 1: Amino Acids, Protein Structure, and Enzymes (Questions 1-35)
1. The peptide bond has partial double-bond character due to:
A) Hydrogen bonding between C=O and N-H
B) Resonance stabilization ✓
C) Steric hindrance from side chains
D) Ionic interactions in the backbone
2. At a pH of 7.0, which amino acid side chain is most likely to be protonated and carry a
positive charge?
A) Glutamate (pKa ~4.2)
B) Histidine (pKa ~6.0) ✓
C) Cysteine (pKa ~8.3)
D) Tyrosine (pKa ~10.1)
3. The α-helix is primarily stabilized by:
A) Disulfide bonds
B) Hydrophobic interactions
C) Hydrogen bonds between backbone C=O and N-H groups four residues apart ✓
D) Ionic bonds between opposite charges
4. In the Michaelis-Menten equation, Km represents:
A) The maximum velocity of the reaction
B) The substrate concentration at 1/2 Vmax ✓
C) The turnover number of the enzyme
D) The enzyme concentration
5. A competitive inhibitor of an enzyme:
A) Binds only to the ES complex
B) Increases the apparent Km without affecting Vmax ✓
C) Decreases the apparent Vmax without affecting Km
D) Alters the enzyme's tertiary structure permanently
,6. The isoelectric point (pI) of an amino acid is the pH at which it:
A) Has maximum buffering capacity
B) Is fully deprotonated
C) Has a net charge of zero ✓
D) Migrates fastest in an electric field
7. In a plot of 1/V vs. 1/[S] (Lineweaver-Burk), a noncompetitive inhibitor will cause:
A) The slope to increase and the y-intercept to remain the same
B) The slope to remain the same and the y-intercept to increase
C) Both the slope and the y-intercept to increase ✓
D) The slope to increase and the y-intercept to decrease
8. Chymotrypsin preferentially cleaves peptide bonds on the carbonyl side of amino acids
with large, hydrophobic side chains due to its:
A) Catalytic triad
B) Oxyanion hole
C) Hydrophobic pocket (S1 pocket) ✓
D) Proximity effect
9. Anfinsen's experiment with ribonuclease demonstrated that:
A) Enzymes require cofactors
B) The primary structure dictates the tertiary structure ✓
C) Disulfide bonds are unnecessary for function
D) Protein folding is always assisted by chaperones
10. Which level of protein structure is defined by the sequence of amino acids?
A) Primary ✓
B) Secondary
C) Tertiary
D) Quaternary
11. An allosteric enzyme regulated by feedback inhibition typically has:
A) Michaelis-Menten kinetics
B) A hyperbolic velocity vs. [S] curve
C) Multiple subunits and a sigmoidal velocity vs. [S] curve ✓
D) A single active site
12. Which pair of amino acids can form a disulfide bridge?
A) Serine and Threonine
B) Lysine and Aspartate
,C) Two Cysteine residues ✓
D) Methionine and Alanine
13. The catalytic mechanism of chymotrypsin involves the formation of a short-lived covalent
intermediate called:
A) A Schiff base
B) An acyl-enzyme intermediate ✓
C) A phosphorylated histidine
D) A gem-diol
14. In hemoglobin, the binding of oxygen to one heme group increases the affinity for oxygen
in the remaining heme groups. This is called:
A) Allosteric inhibition
B) Michaelis-Menten kinetics
C) Cooperative binding ✓
D) Competitive inhibition
15. A zymogen is:
A) A vitamin precursor
B) An inactive enzyme precursor ✓
C) A type of prosthetic group
D) An allosteric activator
16. The β-pleated sheet is an example of:
A) Primary structure
B) Secondary structure ✓
C) Tertiary structure
D) Quaternary structure
17. Which amino acid is most likely to be found in the interior of a globular protein in aqueous
solution?
A) Leucine ✓
B) Aspartic Acid
C) Lysine
D) Serine
18. In the reaction catalyzed by lysozyme, the intermediate formed is a:
A) Covalent glycosyl-enzyme intermediate ✓
B) Phosphorylated histidine
, C) Tetrahedral intermediate
D) Acyl-enzyme intermediate
19. The Bohr effect describes:
A) The decrease in hemoglobin's oxygen affinity at lower pH ✓
B) The cooperative binding of oxygen
C) The mechanism of carbonic anhydrase
D) The folding of β-sheets
20. Which is NOT a mechanism of enzyme catalysis?
A) General acid-base catalysis
B) Covalent catalysis
C) Induced fit
D) Reducing the activation energy by changing the equilibrium of the reaction ✓
21. A protein with a quaternary structure must have:
A) At least two polypeptide chains ✓
B) A prosthetic group
C) Disulfide bonds
D) An α-helical motif
22. Myoglobin has a hyperbolic oxygen-binding curve because it:
A) Binds oxygen cooperatively
B) Is a single-subunit protein with a single heme group ✓
C) Is regulated by 2,3-BPG
D) Contains iron in the Fe³⁺ state
23. 2,3-Bisphosphoglycerate (2,3-BPG):
A) Increases hemoglobin's affinity for oxygen
B) Binds to the heme iron
C) Stabilizes the T (tense) state of hemoglobin, decreasing oxygen affinity ✓
D) Is a key intermediate in glycolysis
24. The coenzyme NAD+ is primarily involved in reactions involving:
A) Group transfer
B) Oxidation-reduction ✓
C) Decarboxylation
D) Transamination
25. Which technique would be best for determining the three-dimensional structure of a
protein at atomic resolution?
COMPLETE CONCEPT REVIEW & PRACTICE
MATERIALS (LATEST EDITION)
Biochemistry 210: Final Exam Practice Questions
Section 1: Amino Acids, Protein Structure, and Enzymes (Questions 1-35)
1. The peptide bond has partial double-bond character due to:
A) Hydrogen bonding between C=O and N-H
B) Resonance stabilization ✓
C) Steric hindrance from side chains
D) Ionic interactions in the backbone
2. At a pH of 7.0, which amino acid side chain is most likely to be protonated and carry a
positive charge?
A) Glutamate (pKa ~4.2)
B) Histidine (pKa ~6.0) ✓
C) Cysteine (pKa ~8.3)
D) Tyrosine (pKa ~10.1)
3. The α-helix is primarily stabilized by:
A) Disulfide bonds
B) Hydrophobic interactions
C) Hydrogen bonds between backbone C=O and N-H groups four residues apart ✓
D) Ionic bonds between opposite charges
4. In the Michaelis-Menten equation, Km represents:
A) The maximum velocity of the reaction
B) The substrate concentration at 1/2 Vmax ✓
C) The turnover number of the enzyme
D) The enzyme concentration
5. A competitive inhibitor of an enzyme:
A) Binds only to the ES complex
B) Increases the apparent Km without affecting Vmax ✓
C) Decreases the apparent Vmax without affecting Km
D) Alters the enzyme's tertiary structure permanently
,6. The isoelectric point (pI) of an amino acid is the pH at which it:
A) Has maximum buffering capacity
B) Is fully deprotonated
C) Has a net charge of zero ✓
D) Migrates fastest in an electric field
7. In a plot of 1/V vs. 1/[S] (Lineweaver-Burk), a noncompetitive inhibitor will cause:
A) The slope to increase and the y-intercept to remain the same
B) The slope to remain the same and the y-intercept to increase
C) Both the slope and the y-intercept to increase ✓
D) The slope to increase and the y-intercept to decrease
8. Chymotrypsin preferentially cleaves peptide bonds on the carbonyl side of amino acids
with large, hydrophobic side chains due to its:
A) Catalytic triad
B) Oxyanion hole
C) Hydrophobic pocket (S1 pocket) ✓
D) Proximity effect
9. Anfinsen's experiment with ribonuclease demonstrated that:
A) Enzymes require cofactors
B) The primary structure dictates the tertiary structure ✓
C) Disulfide bonds are unnecessary for function
D) Protein folding is always assisted by chaperones
10. Which level of protein structure is defined by the sequence of amino acids?
A) Primary ✓
B) Secondary
C) Tertiary
D) Quaternary
11. An allosteric enzyme regulated by feedback inhibition typically has:
A) Michaelis-Menten kinetics
B) A hyperbolic velocity vs. [S] curve
C) Multiple subunits and a sigmoidal velocity vs. [S] curve ✓
D) A single active site
12. Which pair of amino acids can form a disulfide bridge?
A) Serine and Threonine
B) Lysine and Aspartate
,C) Two Cysteine residues ✓
D) Methionine and Alanine
13. The catalytic mechanism of chymotrypsin involves the formation of a short-lived covalent
intermediate called:
A) A Schiff base
B) An acyl-enzyme intermediate ✓
C) A phosphorylated histidine
D) A gem-diol
14. In hemoglobin, the binding of oxygen to one heme group increases the affinity for oxygen
in the remaining heme groups. This is called:
A) Allosteric inhibition
B) Michaelis-Menten kinetics
C) Cooperative binding ✓
D) Competitive inhibition
15. A zymogen is:
A) A vitamin precursor
B) An inactive enzyme precursor ✓
C) A type of prosthetic group
D) An allosteric activator
16. The β-pleated sheet is an example of:
A) Primary structure
B) Secondary structure ✓
C) Tertiary structure
D) Quaternary structure
17. Which amino acid is most likely to be found in the interior of a globular protein in aqueous
solution?
A) Leucine ✓
B) Aspartic Acid
C) Lysine
D) Serine
18. In the reaction catalyzed by lysozyme, the intermediate formed is a:
A) Covalent glycosyl-enzyme intermediate ✓
B) Phosphorylated histidine
, C) Tetrahedral intermediate
D) Acyl-enzyme intermediate
19. The Bohr effect describes:
A) The decrease in hemoglobin's oxygen affinity at lower pH ✓
B) The cooperative binding of oxygen
C) The mechanism of carbonic anhydrase
D) The folding of β-sheets
20. Which is NOT a mechanism of enzyme catalysis?
A) General acid-base catalysis
B) Covalent catalysis
C) Induced fit
D) Reducing the activation energy by changing the equilibrium of the reaction ✓
21. A protein with a quaternary structure must have:
A) At least two polypeptide chains ✓
B) A prosthetic group
C) Disulfide bonds
D) An α-helical motif
22. Myoglobin has a hyperbolic oxygen-binding curve because it:
A) Binds oxygen cooperatively
B) Is a single-subunit protein with a single heme group ✓
C) Is regulated by 2,3-BPG
D) Contains iron in the Fe³⁺ state
23. 2,3-Bisphosphoglycerate (2,3-BPG):
A) Increases hemoglobin's affinity for oxygen
B) Binds to the heme iron
C) Stabilizes the T (tense) state of hemoglobin, decreasing oxygen affinity ✓
D) Is a key intermediate in glycolysis
24. The coenzyme NAD+ is primarily involved in reactions involving:
A) Group transfer
B) Oxidation-reduction ✓
C) Decarboxylation
D) Transamination
25. Which technique would be best for determining the three-dimensional structure of a
protein at atomic resolution?
