WGU C785 FINAL EXAM 300 ACTUAL QUESTIONS
AND CORRECT ANSWERS WITH RATIONALE
LATEST UPDATE ALREADY GRADED A+
This comprehensive WGU C785 Final Exam practice guide features 300
unique, multiple-choice questions designed to mirror the biochemistry and
molecular biology content of the WGU C785 exam. Each question includes the
correct answer and a detailed, evidence-based rationale explaining the
underlying biochemical principles, molecular mechanisms, and clinical
applications. The questions comprehensively cover major topics including
protein structure, enzyme kinetics and regulation, DNA replication and
repair, transcription and translation, metabolic pathways (glycolysis, TCA
cycle, oxidative phosphorylation, gluconeogenesis, fatty acid metabolism, and
amino acid metabolism), hormone signaling, genetic disorders, and metabolic
integration. No questions are repeated, ensuring a thorough review of diverse
biochemistry topics. This resource is ideal for WGU nursing students
preparing for the C785 final examination, offering rigorous self-assessment
and knowledge reinforcement across the full spectrum of biochemistry
essential for clinical practice.
Question 1
Which level of protein structure is disrupted through the hydrolysis of peptide
bonds?
A) Quaternary structure
B) Tertiary structure
C) Primary structure
D) Secondary structure
Answer: C) Primary structure
Rationale: The primary structure of a protein is the linear sequence of amino acids
held together by peptide bonds. Peptide bonds are formed by dehydration reactions
and disrupted by hydrolysis. Disruption of peptide bonds directly affects the
primary structure, which in turn affects all higher levels of protein folding.
---
,Question 2
A mutation in the beta-hemoglobin gene results in the replacement of glutamate at
position 6 with valine, leading to sickle cell anemia. The original amino acid in a
healthy patient is glutamate, which is negatively charged. The mutated amino acid
is valine, which is non-polar. If the beta hemoglobin gene in a patient with sickle-
cell anemia were to be edited so that the valine was replaced with a different amino
acid, which replacement would be expected to have the best clinical outcome?
A) Any non-polar amino acid
B) Any polar uncharged amino acid
C) Any positively charged amino acid
D) Any negatively charged amino acid
Answer: D) Any negatively charged amino acid
Rationale: The best amino acid to replace valine so that the patient is healthy again
would be the one most like glutamate, which is negatively charged. The
hydrophobic interaction caused by valine creates the sickle cell phenotype.
Replacing valine with a negatively charged amino acid would restore normal
hemoglobin function.
---
Question 3
Secondary, tertiary, and quaternary levels of protein structure can all be impacted
by exposing a protein to which treatment?
A) Change of a hydrophobic amino acid to a different hydrophobic amino acid
B) Addition of a reducing agent
C) Placement of the protein in a solution with a low pH
D) Increase in the concentration of the protein in solution
Answer: C) Placement of the protein in a solution with a low pH
Rationale: Changes in pH affect hydrogen bonds and ionic bonds. Hydrogen bonds
in the backbone of amino acids occur in secondary structure, and both hydrogen
bonds and ionic bonds occur in the side chains of amino acids in tertiary structure.
Quaternary structure is also impacted because subunit interactions depend on these
same forces.
---
,Question 4
An increase in beta-pleated sheet structure in some brain proteins can lead to an
increase in amyloid deposit formation, characteristic of some neurodegenerative
diseases. What is the primary biochemical process that follows the increase in beta-
pleated sheet structure that leads to the development of the amyloid deposits?
A) An increase in glycogen formation in the brain cells
B) Aggregation of the proteins in the brain
C) Secretion of glucagon, leading to excessive ketogenesis
D) An increase in anaerobic metabolism of glucose in the brain
Answer: B) Aggregation of the proteins in the brain
Rationale: This question describes changes in protein structure. Aggregation
occurs when proteins clump together inappropriately, causing plaques like amyloid
deposits to accumulate. The increase in beta-pleated sheet structure promotes
protein aggregation.
---
Question 5
Which level of protein structure is determined by the sequence of amino acids?
A) Secondary structure
B) Quaternary structure
C) Tertiary structure
D) Primary structure
Answer: D) Primary structure
Rationale: The primary structure of a protein is simply the sequence of amino acids
held together by peptide bonds. This sequence determines all higher levels of
protein structure.
---
Question 6
Which force is most influential in determining the secondary structure of a protein?
A) Hydrophobic effect
B) Disulfide bonding
C) Hydrogen bonding
, D) Electrostatic interactions
Answer: C) Hydrogen bonding
Rationale: The secondary structure of a protein is built by hydrogen bonds between
the carboxyl groups and amino groups on the backbones of the amino acids. These
hydrogen bonds form the alpha helix and beta pleated sheet structures.
---
Question 7
Which amino acid would most likely participate in hydrogen bonds?
A) A non-polar amino acid with only CH groups
B) A polar, uncharged amino acid with an OH group
C) A non-polar amino acid with sulfur
D) A non-polar amino acid with CH3 groups
Answer: B) A polar, uncharged amino acid with an OH group
Rationale: Polar, uncharged amino acids containing oxygen or NH groups can
form hydrogen bonds. The OH group on the side chain provides a hydrogen bond
donor and acceptor.
---
Question 8
Which portion of the amino acid is the variable group that differs between amino
acids?
A) Amino group
B) Carboxyl group
C) Side chain
D) Alpha carbon
Answer: C) Side chain
Rationale: The side chain is the variable group of the amino acid, also called the R
group. Every amino acid has the same amino group, carboxylic acid group, and an
alpha carbon, but the side chain is different for each amino acid.
---
AND CORRECT ANSWERS WITH RATIONALE
LATEST UPDATE ALREADY GRADED A+
This comprehensive WGU C785 Final Exam practice guide features 300
unique, multiple-choice questions designed to mirror the biochemistry and
molecular biology content of the WGU C785 exam. Each question includes the
correct answer and a detailed, evidence-based rationale explaining the
underlying biochemical principles, molecular mechanisms, and clinical
applications. The questions comprehensively cover major topics including
protein structure, enzyme kinetics and regulation, DNA replication and
repair, transcription and translation, metabolic pathways (glycolysis, TCA
cycle, oxidative phosphorylation, gluconeogenesis, fatty acid metabolism, and
amino acid metabolism), hormone signaling, genetic disorders, and metabolic
integration. No questions are repeated, ensuring a thorough review of diverse
biochemistry topics. This resource is ideal for WGU nursing students
preparing for the C785 final examination, offering rigorous self-assessment
and knowledge reinforcement across the full spectrum of biochemistry
essential for clinical practice.
Question 1
Which level of protein structure is disrupted through the hydrolysis of peptide
bonds?
A) Quaternary structure
B) Tertiary structure
C) Primary structure
D) Secondary structure
Answer: C) Primary structure
Rationale: The primary structure of a protein is the linear sequence of amino acids
held together by peptide bonds. Peptide bonds are formed by dehydration reactions
and disrupted by hydrolysis. Disruption of peptide bonds directly affects the
primary structure, which in turn affects all higher levels of protein folding.
---
,Question 2
A mutation in the beta-hemoglobin gene results in the replacement of glutamate at
position 6 with valine, leading to sickle cell anemia. The original amino acid in a
healthy patient is glutamate, which is negatively charged. The mutated amino acid
is valine, which is non-polar. If the beta hemoglobin gene in a patient with sickle-
cell anemia were to be edited so that the valine was replaced with a different amino
acid, which replacement would be expected to have the best clinical outcome?
A) Any non-polar amino acid
B) Any polar uncharged amino acid
C) Any positively charged amino acid
D) Any negatively charged amino acid
Answer: D) Any negatively charged amino acid
Rationale: The best amino acid to replace valine so that the patient is healthy again
would be the one most like glutamate, which is negatively charged. The
hydrophobic interaction caused by valine creates the sickle cell phenotype.
Replacing valine with a negatively charged amino acid would restore normal
hemoglobin function.
---
Question 3
Secondary, tertiary, and quaternary levels of protein structure can all be impacted
by exposing a protein to which treatment?
A) Change of a hydrophobic amino acid to a different hydrophobic amino acid
B) Addition of a reducing agent
C) Placement of the protein in a solution with a low pH
D) Increase in the concentration of the protein in solution
Answer: C) Placement of the protein in a solution with a low pH
Rationale: Changes in pH affect hydrogen bonds and ionic bonds. Hydrogen bonds
in the backbone of amino acids occur in secondary structure, and both hydrogen
bonds and ionic bonds occur in the side chains of amino acids in tertiary structure.
Quaternary structure is also impacted because subunit interactions depend on these
same forces.
---
,Question 4
An increase in beta-pleated sheet structure in some brain proteins can lead to an
increase in amyloid deposit formation, characteristic of some neurodegenerative
diseases. What is the primary biochemical process that follows the increase in beta-
pleated sheet structure that leads to the development of the amyloid deposits?
A) An increase in glycogen formation in the brain cells
B) Aggregation of the proteins in the brain
C) Secretion of glucagon, leading to excessive ketogenesis
D) An increase in anaerobic metabolism of glucose in the brain
Answer: B) Aggregation of the proteins in the brain
Rationale: This question describes changes in protein structure. Aggregation
occurs when proteins clump together inappropriately, causing plaques like amyloid
deposits to accumulate. The increase in beta-pleated sheet structure promotes
protein aggregation.
---
Question 5
Which level of protein structure is determined by the sequence of amino acids?
A) Secondary structure
B) Quaternary structure
C) Tertiary structure
D) Primary structure
Answer: D) Primary structure
Rationale: The primary structure of a protein is simply the sequence of amino acids
held together by peptide bonds. This sequence determines all higher levels of
protein structure.
---
Question 6
Which force is most influential in determining the secondary structure of a protein?
A) Hydrophobic effect
B) Disulfide bonding
C) Hydrogen bonding
, D) Electrostatic interactions
Answer: C) Hydrogen bonding
Rationale: The secondary structure of a protein is built by hydrogen bonds between
the carboxyl groups and amino groups on the backbones of the amino acids. These
hydrogen bonds form the alpha helix and beta pleated sheet structures.
---
Question 7
Which amino acid would most likely participate in hydrogen bonds?
A) A non-polar amino acid with only CH groups
B) A polar, uncharged amino acid with an OH group
C) A non-polar amino acid with sulfur
D) A non-polar amino acid with CH3 groups
Answer: B) A polar, uncharged amino acid with an OH group
Rationale: Polar, uncharged amino acids containing oxygen or NH groups can
form hydrogen bonds. The OH group on the side chain provides a hydrogen bond
donor and acceptor.
---
Question 8
Which portion of the amino acid is the variable group that differs between amino
acids?
A) Amino group
B) Carboxyl group
C) Side chain
D) Alpha carbon
Answer: C) Side chain
Rationale: The side chain is the variable group of the amino acid, also called the R
group. Every amino acid has the same amino group, carboxylic acid group, and an
alpha carbon, but the side chain is different for each amino acid.
---
