WGU C785 Biochemistry OA | QUESTIONS AND ANSWERS | 2025/2026
Which level of protein structure is Primary
disrupted through the hydrolysis of
peptide bonds? 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
Quaternary by hydrolysis.
Tertiary
Primary
Secondary
A mutation in the beta-hemoglobin gene, The original amino acid in a healthy patient is glutamate, which is negatively
which results in the replacement of the charged. The mutated amino acid is valine, which is non-polar. Valine is causing
amino acid glutamate in position 6 with the sickle cell anemia. The best amino acid to replace valine so that the patient is
amino acid valine, leads to the healthy again would be the one most like glutamate, so any negatively charged
development of sickle cell anemia. The amino acid.
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
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 quaternary levels Placement of the protein in a solution with a low pH
of protein structure can all be impacted by
exposing a protein to which treatment? Changes in pH affect hydrogen bonds and ionic bonds. Hydrogen bonds in
the backbone of amino acids occur in secondary structure, and both hydrogen
Change of a hydrophobic amino acid to a bonds and ionic bonds occur in the side chains of amino acids in tertiary
different hydrophobic amino acid structure.
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
An increase in beta-pleated sheet structure Aggregation of the proteins in the brain
in some brain proteins can lead to an
increase in amyloid deposit formation, This question is describing changes in protein structure. Aggregation occurs
characteristic of some neurodegenerative when proteins clump together inappropriately, causing plaques like amyloid
diseases. What is the primary biochemical 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 amino
acids? The primary structure of a protein is simply the sequence of amino acids held
together by peptide bonds.
Secondary
structure
Quaternary structure
Tertiary structure
Primary structure
, Which force is most influential in Hydrogen bonding
determining the secondary structure of a
protein? 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.
Hydrophobic
effect Disulfide
bonding
Hydrogen
bonding
Electrostatic interactions
Amino Acid structure 4
Which amino acid would most likely
participate in hydrogen bonds? This is a polar, uncharged amino acid due 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 inside Side Chain
the box?
The side chain is the variable group of the amino acid, also called the R group.
The box is surrounding the section below Every amino acid has the same amino group, carboxylic acid group, and an alpha
the Alpha Carbon carbon, but the side chain is different.
Both of these amino acids are non-polar and therefore can interact together
Which pair of amino acids will most likely
with a hydrophobic interaction. Please note that the "S" in the amino acid on the right
interact through hydrophobic forces
is non- polar, while the "SH" group in answer choice D is polar. The S must have an
between their side chains?
H to be polar and is otherwise non-polar.
Alpha Carbon
Which portion of the amino acid is inside
the box?
The alpha carbon is the central carbon on an amino acid that holds together
the other groups of the amino acid. It is always attached to the amino group, the
The box is over the Carbon at the Center of
carboxyl group, the side chain, and a single hydrogen. It is part of the backbone
the chain
of the amino acid and is found in every amino acid.
Given the following amino acid Hydrophobic interaction
structure, what is the strongest
intermolecular force it would participate The amino acid pictured only has CH groups in its side chain, and therefore is non-
in to stabilize a protein structure? polar. Non-polar amino acids make hydrophobic interactions.
Ionic bond
Disulfide bond
Hydrogen bond
Hydrophobic interaction
Which level of protein structure is Primary
disrupted through the hydrolysis of
peptide bonds? 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
Quaternary by hydrolysis.
Tertiary
Primary
Secondary
A mutation in the beta-hemoglobin gene, The original amino acid in a healthy patient is glutamate, which is negatively
which results in the replacement of the charged. The mutated amino acid is valine, which is non-polar. Valine is causing
amino acid glutamate in position 6 with the sickle cell anemia. The best amino acid to replace valine so that the patient is
amino acid valine, leads to the healthy again would be the one most like glutamate, so any negatively charged
development of sickle cell anemia. The amino acid.
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
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 quaternary levels Placement of the protein in a solution with a low pH
of protein structure can all be impacted by
exposing a protein to which treatment? Changes in pH affect hydrogen bonds and ionic bonds. Hydrogen bonds in
the backbone of amino acids occur in secondary structure, and both hydrogen
Change of a hydrophobic amino acid to a bonds and ionic bonds occur in the side chains of amino acids in tertiary
different hydrophobic amino acid structure.
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
An increase in beta-pleated sheet structure Aggregation of the proteins in the brain
in some brain proteins can lead to an
increase in amyloid deposit formation, This question is describing changes in protein structure. Aggregation occurs
characteristic of some neurodegenerative when proteins clump together inappropriately, causing plaques like amyloid
diseases. What is the primary biochemical 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 amino
acids? The primary structure of a protein is simply the sequence of amino acids held
together by peptide bonds.
Secondary
structure
Quaternary structure
Tertiary structure
Primary structure
, Which force is most influential in Hydrogen bonding
determining the secondary structure of a
protein? 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.
Hydrophobic
effect Disulfide
bonding
Hydrogen
bonding
Electrostatic interactions
Amino Acid structure 4
Which amino acid would most likely
participate in hydrogen bonds? This is a polar, uncharged amino acid due 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 inside Side Chain
the box?
The side chain is the variable group of the amino acid, also called the R group.
The box is surrounding the section below Every amino acid has the same amino group, carboxylic acid group, and an alpha
the Alpha Carbon carbon, but the side chain is different.
Both of these amino acids are non-polar and therefore can interact together
Which pair of amino acids will most likely
with a hydrophobic interaction. Please note that the "S" in the amino acid on the right
interact through hydrophobic forces
is non- polar, while the "SH" group in answer choice D is polar. The S must have an
between their side chains?
H to be polar and is otherwise non-polar.
Alpha Carbon
Which portion of the amino acid is inside
the box?
The alpha carbon is the central carbon on an amino acid that holds together
the other groups of the amino acid. It is always attached to the amino group, the
The box is over the Carbon at the Center of
carboxyl group, the side chain, and a single hydrogen. It is part of the backbone
the chain
of the amino acid and is found in every amino acid.
Given the following amino acid Hydrophobic interaction
structure, what is the strongest
intermolecular force it would participate The amino acid pictured only has CH groups in its side chain, and therefore is non-
in to stabilize a protein structure? polar. Non-polar amino acids make hydrophobic interactions.
Ionic bond
Disulfide bond
Hydrogen bond
Hydrophobic interaction
