WGU C785 FINAL EXAM | 2026/2027
Western Governors University Biochemistry Final Exam with Complete Questions & All Correct
Answers | Latest Version
Overview
This 2026/2027 updated resource contains the latest WGU C785 Biochemistry Final
Examination with the exact 120 questions and all correct answers, following current WGU College of
Health Professions curriculum standards, evidence-based biochemical principles, and clinical applications
across all molecular and cellular biology domains.
Key Features
● Actual WGU C785 final exam format with the official 120 questions
● Comprehensive coverage of biochemistry principles and clinical correlations
● Updated 2026/2027 biochemical research and medical applications
● Practical clinical scenario applications and diagnostic reasoning
● All correct answers verified with detailed rationales
Core Content Areas (120 Total Questions)
● Biomolecular Structure & Function (25 Qs)
● Enzyme Kinetics & Regulation (20 Qs)
● Metabolic Pathways & Energy Production (25 Qs)
● Molecular Genetics & Protein Synthesis (20 Qs)
● Clinical Biochemistry Applications (20 Qs)
● Laboratory Techniques & Diagnostics (10 Qs)
Detailed Content Breakdown
● Protein Structure & Function Relationships (15 Qs)
● Carbohydrate Metabolism & Disorders (15 Qs)
● Lipid Metabolism & Related Diseases (15 Qs)
● Amino Acid & Nucleotide Metabolism (12 Qs)
● DNA Replication, Repair & Transcription (15 Qs)
● Translation & Post-Translational Modifications (12 Qs)
● Signal Transduction & Cellular Communication (10 Qs)
● Vitamins & Coenzymes in Metabolism (10 Qs)
● Inborn Errors of Metabolism (8 Qs)
● Biochemical Laboratory Methods (8 Qs)
Answer Format
Correct answers are marked in bold green and include:
● WGU C785 course competency applications
● Biochemical mechanism explanations at molecular level
● Clinical correlation rationales and diagnostic interpretations
, ● Metabolic pathway regulation and control mechanisms
● Genetic disorder biochemical basis explanations
● Laboratory test result interpretations and significance
Updates for 2026/2027
● Reflects 2026/2027 WGU College of Health Professions curriculum revisions
● Updated metabolic pathway discoveries and therapeutic applications
● Enhanced pharmacogenomics and personalized medicine integration
● New CRISPR and gene editing biochemical mechanisms
● Revised metabolic syndrome and obesity biochemistry
● Updated laboratory technique advancements and diagnostic applications
● New microbiome-host biochemical interactions
● Revised nutritional biochemistry and micronutrient research
Exam Questions (1–120)
1. Which level of protein structure is stabilized primarily by hydrogen bonds between backbone amide and
carbonyl groups?
A. Primary
B. Secondary
C. Tertiary
D. Quaternary
Rationale: Secondary structure (α-helices and β-sheets) is stabilized by hydrogen bonds between the
carbonyl oxygen and amide hydrogen of the polypeptide backbone. Primary structure is the amino acid
sequence (covalent peptide bonds). Tertiary and quaternary involve side-chain interactions.
2. A patient presents with fatigue, muscle weakness, and lactic acidosis after mild exercise. Laboratory
testing reveals a deficiency in an enzyme that converts pyruvate to acetyl-CoA. Which enzyme is most
likely deficient?
A. Lactate dehydrogenase
B. Pyruvate carboxylase
, C. Pyruvate dehydrogenase
D. Phosphofructokinase-1
Rationale: Pyruvate dehydrogenase (PDH) complex converts pyruvate to acetyl-CoA for entry into the
citric acid cycle. PDH deficiency leads to pyruvate accumulation, which is converted to lactate, causing
lactic acidosis—especially during anaerobic conditions like exercise.
3. Which vitamin acts as a coenzyme for carboxylation reactions and is essential for fatty acid synthesis?
A. Vitamin B1 (Thiamine)
B. Vitamin B2 (Riboflavin)
C. Vitamin B7 (Biotin)
D. Vitamin B9 (Folate)
Rationale: Biotin is a cofactor for carboxylase enzymes, including acetyl-CoA carboxylase (first step in
fatty acid synthesis) and pyruvate carboxylase (gluconeogenesis). Deficiency can cause dermatitis,
alopecia, and neurological symptoms.
4. In the electron transport chain, which complex is responsible for pumping protons and transferring
electrons from ubiquinol to cytochrome c?
A. Complex I
B. Complex II
C. Complex III
D. Complex IV
, Rationale: Complex III (cytochrome bc1 complex) accepts electrons from ubiquinol (QH2) and passes
them to cytochrome c while pumping protons across the inner mitochondrial membrane. Complex I
accepts from NADH; Complex II from FADH2 (succinate); Complex IV reduces O2 to H2O.
5. A mutation in the gene encoding the β-globin subunit results in a valine substitution for glutamic acid
at position 6. This causes hemoglobin to polymerize under low oxygen conditions. What is this condition
called?
A. Thalassemia
B. Sickle cell anemia
C. Hemophilia A
D. Phenylketonuria
Rationale: Sickle cell anemia is caused by a point mutation (GAG → GTG) in the HBB gene, resulting
in hemoglobin S (HbS). Deoxygenated HbS polymerizes, distorting red blood cells into sickle shapes,
causing vaso-occlusion and hemolysis.
6. Which enzyme is allosterically activated by citrate and inhibited by palmitoyl-CoA?
A. Hormone-sensitive lipase
B. Carnitine acyltransferase I
C. Acetyl-CoA carboxylase
D. HMG-CoA reductase
Rationale: Acetyl-CoA carboxylase (ACC) catalyzes the committed step in fatty acid synthesis. Citrate
(indicating abundant energy) activates ACC; palmitoyl-CoA (end product) provides feedback inhibition.
ACC is also regulated by phosphorylation (inactive when phosphorylated by AMPK).
7. During DNA replication, which enzyme synthesizes RNA primers required for DNA polymerase
activity?
Western Governors University Biochemistry Final Exam with Complete Questions & All Correct
Answers | Latest Version
Overview
This 2026/2027 updated resource contains the latest WGU C785 Biochemistry Final
Examination with the exact 120 questions and all correct answers, following current WGU College of
Health Professions curriculum standards, evidence-based biochemical principles, and clinical applications
across all molecular and cellular biology domains.
Key Features
● Actual WGU C785 final exam format with the official 120 questions
● Comprehensive coverage of biochemistry principles and clinical correlations
● Updated 2026/2027 biochemical research and medical applications
● Practical clinical scenario applications and diagnostic reasoning
● All correct answers verified with detailed rationales
Core Content Areas (120 Total Questions)
● Biomolecular Structure & Function (25 Qs)
● Enzyme Kinetics & Regulation (20 Qs)
● Metabolic Pathways & Energy Production (25 Qs)
● Molecular Genetics & Protein Synthesis (20 Qs)
● Clinical Biochemistry Applications (20 Qs)
● Laboratory Techniques & Diagnostics (10 Qs)
Detailed Content Breakdown
● Protein Structure & Function Relationships (15 Qs)
● Carbohydrate Metabolism & Disorders (15 Qs)
● Lipid Metabolism & Related Diseases (15 Qs)
● Amino Acid & Nucleotide Metabolism (12 Qs)
● DNA Replication, Repair & Transcription (15 Qs)
● Translation & Post-Translational Modifications (12 Qs)
● Signal Transduction & Cellular Communication (10 Qs)
● Vitamins & Coenzymes in Metabolism (10 Qs)
● Inborn Errors of Metabolism (8 Qs)
● Biochemical Laboratory Methods (8 Qs)
Answer Format
Correct answers are marked in bold green and include:
● WGU C785 course competency applications
● Biochemical mechanism explanations at molecular level
● Clinical correlation rationales and diagnostic interpretations
, ● Metabolic pathway regulation and control mechanisms
● Genetic disorder biochemical basis explanations
● Laboratory test result interpretations and significance
Updates for 2026/2027
● Reflects 2026/2027 WGU College of Health Professions curriculum revisions
● Updated metabolic pathway discoveries and therapeutic applications
● Enhanced pharmacogenomics and personalized medicine integration
● New CRISPR and gene editing biochemical mechanisms
● Revised metabolic syndrome and obesity biochemistry
● Updated laboratory technique advancements and diagnostic applications
● New microbiome-host biochemical interactions
● Revised nutritional biochemistry and micronutrient research
Exam Questions (1–120)
1. Which level of protein structure is stabilized primarily by hydrogen bonds between backbone amide and
carbonyl groups?
A. Primary
B. Secondary
C. Tertiary
D. Quaternary
Rationale: Secondary structure (α-helices and β-sheets) is stabilized by hydrogen bonds between the
carbonyl oxygen and amide hydrogen of the polypeptide backbone. Primary structure is the amino acid
sequence (covalent peptide bonds). Tertiary and quaternary involve side-chain interactions.
2. A patient presents with fatigue, muscle weakness, and lactic acidosis after mild exercise. Laboratory
testing reveals a deficiency in an enzyme that converts pyruvate to acetyl-CoA. Which enzyme is most
likely deficient?
A. Lactate dehydrogenase
B. Pyruvate carboxylase
, C. Pyruvate dehydrogenase
D. Phosphofructokinase-1
Rationale: Pyruvate dehydrogenase (PDH) complex converts pyruvate to acetyl-CoA for entry into the
citric acid cycle. PDH deficiency leads to pyruvate accumulation, which is converted to lactate, causing
lactic acidosis—especially during anaerobic conditions like exercise.
3. Which vitamin acts as a coenzyme for carboxylation reactions and is essential for fatty acid synthesis?
A. Vitamin B1 (Thiamine)
B. Vitamin B2 (Riboflavin)
C. Vitamin B7 (Biotin)
D. Vitamin B9 (Folate)
Rationale: Biotin is a cofactor for carboxylase enzymes, including acetyl-CoA carboxylase (first step in
fatty acid synthesis) and pyruvate carboxylase (gluconeogenesis). Deficiency can cause dermatitis,
alopecia, and neurological symptoms.
4. In the electron transport chain, which complex is responsible for pumping protons and transferring
electrons from ubiquinol to cytochrome c?
A. Complex I
B. Complex II
C. Complex III
D. Complex IV
, Rationale: Complex III (cytochrome bc1 complex) accepts electrons from ubiquinol (QH2) and passes
them to cytochrome c while pumping protons across the inner mitochondrial membrane. Complex I
accepts from NADH; Complex II from FADH2 (succinate); Complex IV reduces O2 to H2O.
5. A mutation in the gene encoding the β-globin subunit results in a valine substitution for glutamic acid
at position 6. This causes hemoglobin to polymerize under low oxygen conditions. What is this condition
called?
A. Thalassemia
B. Sickle cell anemia
C. Hemophilia A
D. Phenylketonuria
Rationale: Sickle cell anemia is caused by a point mutation (GAG → GTG) in the HBB gene, resulting
in hemoglobin S (HbS). Deoxygenated HbS polymerizes, distorting red blood cells into sickle shapes,
causing vaso-occlusion and hemolysis.
6. Which enzyme is allosterically activated by citrate and inhibited by palmitoyl-CoA?
A. Hormone-sensitive lipase
B. Carnitine acyltransferase I
C. Acetyl-CoA carboxylase
D. HMG-CoA reductase
Rationale: Acetyl-CoA carboxylase (ACC) catalyzes the committed step in fatty acid synthesis. Citrate
(indicating abundant energy) activates ACC; palmitoyl-CoA (end product) provides feedback inhibition.
ACC is also regulated by phosphorylation (inactive when phosphorylated by AMPK).
7. During DNA replication, which enzyme synthesizes RNA primers required for DNA polymerase
activity?
