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WGU C785 Biochemistry Unit Exam Questions with Complete Solutions | Fully Updated Study Guide for Western Governors University

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This resource contains the complete WGU C785 Biochemistry unit exam questions with fully solved and verified answers. Designed for Western Governors University students, it covers key biochemistry concepts including macromolecules, enzymes, metabolic pathways, DNA/RNA structure, protein synthesis, and biochemical regulation. Perfect for mastering course content, preparing for assessments, and building confidence before the final exam, this guide ensures you are ready to succeed in the C785 course.

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WGU C785 Biochemistry Unit Exam
Questions fully solved & updated



Which level of protein structure is disrupted through the hydrolysis of
peptide bonds?


Quaternary


Tertiary


Primary


Secondary - ANSWER-Primary


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.


A mutation in the beta-hemoglobin gene, which results in the
replacement of the amino acid glutamate in position 6 with the
amino acid valine, leads to the development of sickle cell anemia.
The structures of glutamate and valine are shown below.


If the beta hemoglobin gene in a patient with sickle-cell anemia were
to be edited so that the valine in position 6 was replaced with a
different amino acid, which replacement for valine would be

, WGU C785 Biochemistry Unit Exam
Questions fully solved & updated



expected to have the best clinical outcome, in theory, for the patient?
(Assume the valine can potentially be replaced with any amino acid
other than glutamate.) - ANSWER-The original amino acid in a
healthy patient is glutamate, which is negatively charged. The
mutated amino acid is valine, which is non-polar. Valine is causing
sickle cell anemia. The best amino acid to replace valine so that the
patient is healthy again would be the one most like glutamate, so any
negatively charged amino acid.


Secondary, tertiary, and quaternary levels of protein structure can all
be impacted by exposing a protein to which treatment?


Change of a hydrophobic amino acid to a different hydrophobic
amino acid


Addition of a reducing agent


Placement of the protein in a solution with a low pH


Increase in the concentration of the protein in solution - ANSWER-
Placement of the protein in a solution with a low pH


Changes in pH affect hydrogen bonds and ionic bonds. Hydrogen
bonds in the backbone of amino acids occur in secondary structure,

, WGU C785 Biochemistry Unit Exam
Questions fully solved & updated



and both hydrogen bonds and ionic bonds occur in the side chains of
amino acids in tertiary structure.


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?


An increase in glycogen formation in the brain cells


Aggregation of the proteins in the brain


Secretion of glucagon, leading to excessive ketogenesis


An increase in anaerobic metabolism of glucose in the brain -
ANSWER-Aggregation of the proteins in the brain


This question is describing changes in protein structure. Aggregation
occurs when proteins clump together inappropriately, causing
plaques like amyloid deposits to accumulate.

, WGU C785 Biochemistry Unit Exam
Questions fully solved & updated



Which level of protein structure is determined by the sequence of
amino acids?


Secondary structure


Quaternary structure


Tertiary structure


Primary structure - ANSWER-Primary structure


The primary structure of a protein is simply the sequence of amino
acids held together by peptide bonds.


Which force is most influential in determining the secondary
structure of a protein?


Hydrophobic effect


Disulfide bonding

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