WGU C785 Final Exam 2024 With All The Correct Answers.
INTRODUCTION
This comprehensive study guide is designed for Western Governors University (WGU) students
preparing for theC785 Biochemistry Final Examfor the 2024/2025 academic cycle. The exam covers
core biochemistry topics including protein structure and folding, enzyme function and inhibition,
metabolism and energy production, DNA replication and repair, transcription and translation, and
genetic mutations.
KEY CONCEPTS REFERENCE GUIDE
Protein Structure & Amino Acids
Q: What is the basic structure of an amino acid?
Answer:Amino group (NH₂ or NH₃⁺), carboxyl group (COO⁻ or COOH), alpha carbon (C), and a
variable R group (side chain)
.
Q: How do you identify the three different types of side chains?
Answer:
• Non-polar/hydrophobic- ends with CH (or "can't have" water)
• Polar - ends with OH, SH, or NH
• Charged- ends with a positive or negative charge
Q: What are the 4 levels of protein structure?
Answer:
1. Primary - linear chain of amino acids held by peptide bonds (covalent)
2. Secondary- folded into alpha helix or beta sheet caused by hydrogen bonding
3. Tertiary - 3D structure caused by side chain (R group) interactions
4. Quaternary- multiple polypeptide chains combine into one functional protein
, Q: What environmental change breaks each type of bond?
Answer:
• Hydrophobic bonds- temperature change
• Ionic bonds- salt or decreased pH
• Hydrogen bonds- temperature change, pH change
• Disulfide bonds- reducing agents
Q: Which level of protein structure is disrupted through the hydrolysis of peptide bonds?
Answer:Primary structure
Rationale: The primary structure of a protein is the sequence of amino acids held together by peptide
bonds. Peptide bonds are formed by dehydration reactions and disrupted by hydrolysis.
Q: Which level of protein structure would be unaffected by complete denaturation of-subunit
a multi
protein?
Answer:Primary structure
Rationale: Peptide bonds are strong covalent bonds. The primary structure is located at the backbone and
does not denature.
Protein Misfolding & Disease
Q: Describe what causes the misfolding of protein in Alzheimer's Disease.
Answer:Protein misfolding is caused by intracellular tangles and extracellular plaques (senile plaques)
caused by abnormal protein aggregation. TAU is fibrous material inside cells where connections are lost,
becoming defective and forming filaments in the neuro
n. Amyloid-beta is a large precursor protein in
the cell; excess amyloid
-beta creates senile plaques. This starts in the hippocampus and moves upward
.
Q: What type of amino acid side chain leads to protein aggregation?
Answer:Hydrophobic bonds
Q: What are the molecules that help denatured proteins with folding?
Answer:Molecular chaperones are protein helpers. They bind to the newly made polypeptide and enable
proper folding. Proper protein folding is vital because proteins that do not fold properly can lead to a
variety of diseases
.
INTRODUCTION
This comprehensive study guide is designed for Western Governors University (WGU) students
preparing for theC785 Biochemistry Final Examfor the 2024/2025 academic cycle. The exam covers
core biochemistry topics including protein structure and folding, enzyme function and inhibition,
metabolism and energy production, DNA replication and repair, transcription and translation, and
genetic mutations.
KEY CONCEPTS REFERENCE GUIDE
Protein Structure & Amino Acids
Q: What is the basic structure of an amino acid?
Answer:Amino group (NH₂ or NH₃⁺), carboxyl group (COO⁻ or COOH), alpha carbon (C), and a
variable R group (side chain)
.
Q: How do you identify the three different types of side chains?
Answer:
• Non-polar/hydrophobic- ends with CH (or "can't have" water)
• Polar - ends with OH, SH, or NH
• Charged- ends with a positive or negative charge
Q: What are the 4 levels of protein structure?
Answer:
1. Primary - linear chain of amino acids held by peptide bonds (covalent)
2. Secondary- folded into alpha helix or beta sheet caused by hydrogen bonding
3. Tertiary - 3D structure caused by side chain (R group) interactions
4. Quaternary- multiple polypeptide chains combine into one functional protein
, Q: What environmental change breaks each type of bond?
Answer:
• Hydrophobic bonds- temperature change
• Ionic bonds- salt or decreased pH
• Hydrogen bonds- temperature change, pH change
• Disulfide bonds- reducing agents
Q: Which level of protein structure is disrupted through the hydrolysis of peptide bonds?
Answer:Primary structure
Rationale: The primary structure of a protein is the sequence of amino acids held together by peptide
bonds. Peptide bonds are formed by dehydration reactions and disrupted by hydrolysis.
Q: Which level of protein structure would be unaffected by complete denaturation of-subunit
a multi
protein?
Answer:Primary structure
Rationale: Peptide bonds are strong covalent bonds. The primary structure is located at the backbone and
does not denature.
Protein Misfolding & Disease
Q: Describe what causes the misfolding of protein in Alzheimer's Disease.
Answer:Protein misfolding is caused by intracellular tangles and extracellular plaques (senile plaques)
caused by abnormal protein aggregation. TAU is fibrous material inside cells where connections are lost,
becoming defective and forming filaments in the neuro
n. Amyloid-beta is a large precursor protein in
the cell; excess amyloid
-beta creates senile plaques. This starts in the hippocampus and moves upward
.
Q: What type of amino acid side chain leads to protein aggregation?
Answer:Hydrophobic bonds
Q: What are the molecules that help denatured proteins with folding?
Answer:Molecular chaperones are protein helpers. They bind to the newly made polypeptide and enable
proper folding. Proper protein folding is vital because proteins that do not fold properly can lead to a
variety of diseases
.
