9/28/25, 3:14 PM
WGU Biochemistry EXAM 2025-2026 \COMPLETE
QUESTIONS AND ACCURATE DETAILED ANSWERS
\VERIFIED 100% ALREADY GRADEDC A+ \LATEST
UPDATE 2025-2026
Assuming 100% reaction 16
efficiency, how many DNA
copies are created after the
completion of four complete
PCR cycles?
What is the function of DNA It recognizes the primers and uses the available dNTPs
polymerase in the process to replicate the template DNA sequence
of PCR?
What type of mutation occurs Nonsense
when
cytosine is completely
mutated to guanin in the
DNA sequence?
When using heat to Hydrophobic interactions
denature a protein, which
force is the first to be
disrupted as temperature
increases?
Which term describes the Primary structure
order of amino acids in a
peptide chain?
/ 1/18
,9/28/25, 11:46 PM WGU Biochemistry
A commonly used technique hydrophobic interactions
for protein
denaturation is adding an acid
or a base to dramatically
change the pH.
Which force is most
impacted by this change in
pH?
In which situation could a A mutation in aconitase blocks an essential step in aerobic
body function be disrupted metabolism
by altering protein
structure?
A mutation replaces an isoleucine with an aspartic acid
How can an alteration in
in a transcription factor protein, which blocks the
protein structure lead to a
normal folding of the protein and its function in the
disease state?
expression of certain genes.
Which structural level Tertiary
shows the greatest
difference when
comparing denatured
proteins with the normal
version of the protein?
Frying an egg changes the Hydrophobic interactions form between denatured egg white
egg white from a clear proteins.
liquid to an opaque solid.
Which molecular change in
the albumin
protein causes this change in
appearance?
What is the driving Propagation of misfolding from one protein to another
mechanism of plaque
formation in prion
diseases?
Which feature of a protein Three-dimensional structure
made of a single polypeptide
/ 2/18
, 9/28/25, 11:46 PM WGU Biochemistry
chain is most directly
responsible for its function?
How does the Bohr effect An increase in carbon dioxide production leads to a
describe the relationship decrease in blood pH, causing hemoglobin to release
between carbon dioxide oxygen more readily.
levels, blood pH and the
amount of oxygen bound
to hemoglobin?
Which statement describes The binding of oxygen gas to heme changes the structure of the
the binding of oxygen gas to heme group.
a heme group?
Which characteristic of It has a high affinity for oxygen.
myoglobin makes it an
effective oxygen storage
molecule?
At low O 2 concentrations, Myoglobin has a much greater affinity for O 2 than hemoglobin
how does myoglobin's does.
affinity for O 2 relate to
hemoglobin's affinity for O
2?
How does pH level When pH lowers, excess H + binds to negatively charged
promote the side chains on hemoglobin and changes ionic bonds
deoxygenated between subunits to favor the T-state
conformation of
hemoglobin?
What is occurring in The amount of carbon dioxide decreases.
surrounding tissues as the
amount of hemoglobin
saturated with oxygen
increases?
Reversible, noncompetitive inhibition of an enzyme in a
What is feedback inhibition?
pathway by a product of that pathway
Which form of enzyme Feedback inhibition
regulation is likely to be
used by an organism to
control the
/ 3/18
WGU Biochemistry EXAM 2025-2026 \COMPLETE
QUESTIONS AND ACCURATE DETAILED ANSWERS
\VERIFIED 100% ALREADY GRADEDC A+ \LATEST
UPDATE 2025-2026
Assuming 100% reaction 16
efficiency, how many DNA
copies are created after the
completion of four complete
PCR cycles?
What is the function of DNA It recognizes the primers and uses the available dNTPs
polymerase in the process to replicate the template DNA sequence
of PCR?
What type of mutation occurs Nonsense
when
cytosine is completely
mutated to guanin in the
DNA sequence?
When using heat to Hydrophobic interactions
denature a protein, which
force is the first to be
disrupted as temperature
increases?
Which term describes the Primary structure
order of amino acids in a
peptide chain?
/ 1/18
,9/28/25, 11:46 PM WGU Biochemistry
A commonly used technique hydrophobic interactions
for protein
denaturation is adding an acid
or a base to dramatically
change the pH.
Which force is most
impacted by this change in
pH?
In which situation could a A mutation in aconitase blocks an essential step in aerobic
body function be disrupted metabolism
by altering protein
structure?
A mutation replaces an isoleucine with an aspartic acid
How can an alteration in
in a transcription factor protein, which blocks the
protein structure lead to a
normal folding of the protein and its function in the
disease state?
expression of certain genes.
Which structural level Tertiary
shows the greatest
difference when
comparing denatured
proteins with the normal
version of the protein?
Frying an egg changes the Hydrophobic interactions form between denatured egg white
egg white from a clear proteins.
liquid to an opaque solid.
Which molecular change in
the albumin
protein causes this change in
appearance?
What is the driving Propagation of misfolding from one protein to another
mechanism of plaque
formation in prion
diseases?
Which feature of a protein Three-dimensional structure
made of a single polypeptide
/ 2/18
, 9/28/25, 11:46 PM WGU Biochemistry
chain is most directly
responsible for its function?
How does the Bohr effect An increase in carbon dioxide production leads to a
describe the relationship decrease in blood pH, causing hemoglobin to release
between carbon dioxide oxygen more readily.
levels, blood pH and the
amount of oxygen bound
to hemoglobin?
Which statement describes The binding of oxygen gas to heme changes the structure of the
the binding of oxygen gas to heme group.
a heme group?
Which characteristic of It has a high affinity for oxygen.
myoglobin makes it an
effective oxygen storage
molecule?
At low O 2 concentrations, Myoglobin has a much greater affinity for O 2 than hemoglobin
how does myoglobin's does.
affinity for O 2 relate to
hemoglobin's affinity for O
2?
How does pH level When pH lowers, excess H + binds to negatively charged
promote the side chains on hemoglobin and changes ionic bonds
deoxygenated between subunits to favor the T-state
conformation of
hemoglobin?
What is occurring in The amount of carbon dioxide decreases.
surrounding tissues as the
amount of hemoglobin
saturated with oxygen
increases?
Reversible, noncompetitive inhibition of an enzyme in a
What is feedback inhibition?
pathway by a product of that pathway
Which form of enzyme Feedback inhibition
regulation is likely to be
used by an organism to
control the
/ 3/18
