CHEM 210 BIOCHEMISTRY MODULE 2
AND FINAL EXAM ADVANCED
PRACTICE QUESTIONS AND ANSWERS
2026/2027 UPDATE || 100% GUARANTEED
PASS
1. Which of the following amino acids lacks a chiral center at the alpha-carbon?
A. Glycine
B. Alanine
C. Proline
D. Serine
Answer: A
Conceptual Explanation: Glycine’s R-group is a hydrogen atom, making the alpha-carbon
bonded to two identical groups (H), thus it is achiral.
2. What characterizes the ‘partial double bond’ nature of a peptide bond?
A. Free rotation around the C-N bond
B. The presence of a triple bond between Carbon and Nitrogen
C. Ionic interaction between adjacent amino acids
D. Resonance between the carbonyl oxygen and the amide nitrogen
,Answer: D
Conceptual Explanation: Resonance in the peptide bond gives the C-N bond about 40%
double-bond character, restricting rotation and keeping the group planar.
3. In an alpha-helix, the hydrogen bonds occur between which groups?
A. Between R-groups of every 3rd residue
B. Between the C=O of residue i and the N-H of residue i+4
C. Between the N-H of residue i and the C=O of residue i+3
D. Between the C=O of residue i and the C=O of residue i+4
Answer: B
Conceptual Explanation: The alpha-helix is stabilized by intrachain hydrogen bonds
between the carbonyl oxygen of one amino acid and the amide hydrogen four residues
ahead.
4. Which amino acid is known as a ‘helix breaker’ due to its rigid cyclic structure?
A. Tryptophan
B. Histidine
C. Proline
D. Leucine
Answer: C
, Conceptual Explanation: Proline’s nitrogen is part of a five-membered ring, which limits
its phi angle and prevents it from participating in the standard alpha-helix H-bonding
pattern.
5. What is the primary driving force behind the folding of globular proteins?
A. Metal ion coordination
B. Disulfide bond formation
C. Ionic ‘salt bridges’
D. The hydrophobic effect
Answer: D
Conceptual Explanation: The release of water molecules from structured ‘clathrate’ cages
around nonpolar side chains (increasing entropy) drives the hydrophobic groups to the
interior.
6. A solution of an amino acid is at a pH where it carries no net charge. This pH is called the:
A. Isoelectric point (pI)
B. Zwitterion point
C. Equilibrium constant
D. Dissociation constant
Answer: A
AND FINAL EXAM ADVANCED
PRACTICE QUESTIONS AND ANSWERS
2026/2027 UPDATE || 100% GUARANTEED
PASS
1. Which of the following amino acids lacks a chiral center at the alpha-carbon?
A. Glycine
B. Alanine
C. Proline
D. Serine
Answer: A
Conceptual Explanation: Glycine’s R-group is a hydrogen atom, making the alpha-carbon
bonded to two identical groups (H), thus it is achiral.
2. What characterizes the ‘partial double bond’ nature of a peptide bond?
A. Free rotation around the C-N bond
B. The presence of a triple bond between Carbon and Nitrogen
C. Ionic interaction between adjacent amino acids
D. Resonance between the carbonyl oxygen and the amide nitrogen
,Answer: D
Conceptual Explanation: Resonance in the peptide bond gives the C-N bond about 40%
double-bond character, restricting rotation and keeping the group planar.
3. In an alpha-helix, the hydrogen bonds occur between which groups?
A. Between R-groups of every 3rd residue
B. Between the C=O of residue i and the N-H of residue i+4
C. Between the N-H of residue i and the C=O of residue i+3
D. Between the C=O of residue i and the C=O of residue i+4
Answer: B
Conceptual Explanation: The alpha-helix is stabilized by intrachain hydrogen bonds
between the carbonyl oxygen of one amino acid and the amide hydrogen four residues
ahead.
4. Which amino acid is known as a ‘helix breaker’ due to its rigid cyclic structure?
A. Tryptophan
B. Histidine
C. Proline
D. Leucine
Answer: C
, Conceptual Explanation: Proline’s nitrogen is part of a five-membered ring, which limits
its phi angle and prevents it from participating in the standard alpha-helix H-bonding
pattern.
5. What is the primary driving force behind the folding of globular proteins?
A. Metal ion coordination
B. Disulfide bond formation
C. Ionic ‘salt bridges’
D. The hydrophobic effect
Answer: D
Conceptual Explanation: The release of water molecules from structured ‘clathrate’ cages
around nonpolar side chains (increasing entropy) drives the hydrophobic groups to the
interior.
6. A solution of an amino acid is at a pH where it carries no net charge. This pH is called the:
A. Isoelectric point (pI)
B. Zwitterion point
C. Equilibrium constant
D. Dissociation constant
Answer: A
