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Exam (elaborations)

WGU C785 Biochemistry Unit Exam Questions and Answers with Verified Solutions | Latest Updated 2026

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WGU C785 Biochemistry Unit Exam Questions and Answers with Verified Solutions | Latest Updated 2026

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WGU C785 Biochemistry Unit Exam
Questions and Answers with Verified
Solutions | Latest Updated 2026



Which level of protein structure is Primary
disrupted through the hydrolysis of The primary structure of a protein is the
peptide bonds? sequence
Quaternary of amino acids held together by peptide
Tertiary bonds.
Primary Peptide bonds are formed by dehydration
Secondary reactions and disrupted by hydrolysis.


A mutation in the beta-hemoglobin The original amino acid in a healthy patient
gene, which results in the is
replacement of the amino acid glutamate, which is negatively charged.
glutamate in position 6 with the The
amino acid valine, leads to the mutated amino acid is valine, which is
development of sickle cell anemia. non-polar.
The structures of glutamate and Valine is causing sickle cell anemia. The
valine are shown below. best amino
If the beta hemoglobin gene in a acid to replace valine so that the patient is
patient with sickle-cell anemia healthy
were again would be the one most like
to be edited so that the valine in glutamate, so any
position 6 was replaced with a negatively charged amino acid.
different amino acid, which
replacement for valine would be
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.)

,Secondary, tertiary, and Placement of the protein in a solution with
quaternary a low
levels of protein structure can all pH
be Changes in pH affect hydrogen bonds and
impacted by exposing a protein to ionic
which treatment? bonds. Hydrogen bonds in the backbone of
Change of a hydrophobic amino amino
acid acids occur in secondary structure, and
to a different hydrophobic amino both
acid hydrogen bonds and ionic bonds occur in
Addition of a reducing agent the side
Placement of the protein in a chains of amino acids in tertiary structure.
solution with a low pH
Increase in the concentration of
the
protein in solution

,An increase in beta-pleated sheet Aggregation of the proteins in the brain
structure in some brain proteins This question is describing changes in
can protein
lead to an increase in amyloid structure. Aggregation occurs when
deposit formation, characteristic of proteins clump
some neurodegenerative together inappropriately, causing plaques
diseases. like
What is the primary biochemical amyloid deposits to accumulate.
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


Which level of protein structure is Primary structure
determined by the sequence of The primary structure of a protein is simply
amino acids? the
Secondary structure sequence of amino acids held together by
Quaternary structure peptide
Tertiary structure bonds.
Primary structure

, Which force is most influential in Hydrogen bonding
determining the secondary The secondary structure of a protein is
structure built by
of a protein? hydrogen bonds between the carboxyl
Hydrophobic effect groups and
Disulfide bonding amino groups on the backbones of the
Hydrogen bonding amino
Electrostatic interactions acids.


Which amino acid would most Amino Acid structure 4
likely This is a polar, uncharged amino acid due
participate in hydrogen bonds? to the
OH group on the side chain. Polar,
uncharged
amino acids containing oxygen or NH
groups make
hydrogen bonds.


Which portion of the amino acid is Side Chain
inside the box? The side chain is the variable group of the
The box is surrounding the section amino
below the Alpha Carbon 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.

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