WGU C785 Biochemistry Unit Exam Questions
Study online at https://quizlet.com/_hseauw
1. Which level of protein structure is dis- Primary
rupted through the hydrolysis of pep-
tide bonds? The primary structure of a protein is the se-
quence of amino acids held together by peptide
Quaternary bonds. Peptide bonds are formed by dehydra-
tion reactions and disrupted by hydrolysis.
Tertiary
Primary
Secondary
2. A mutation in the beta-hemoglobin The original amino acid in a healthy patient is
gene, which results in the replacement glutamate, which is negatively charged. The mu-
of the amino acid glutamate in position tated amino acid is valine, which is non-polar. Va-
6 with the amino acid valine, leads to line is causing sickle cell anemia. The best amino
the development of sickle cell anemia. acid to replace valine so that the patient is healthy
The structures of glutamate and valine again would be the one most like glutamate, so
are shown below. any negatively charged amino acid.
If the beta hemoglobin gene in a patient
with sickle-cell anemia were to be edit-
ed 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 out-
come, in theory, for the patient? (As-
sume the valine can potentially be re-
placed with any amino acid other than
glutamate.)
3. Secondary, tertiary, and quaternary lev- Placement of the protein in a solution with a low
els of protein structure can all be im- pH
, WGU C785 Biochemistry Unit Exam Questions
Study online at https://quizlet.com/_hseauw
pacted by exposing a protein to which
treatment? Changes in pH affect hydrogen bonds and ion-
ic bonds. Hydrogen bonds in the backbone of
Change of a hydrophobic amino acid to amino acids occur in secondary structure, and
a different hydrophobic amino acid both hydrogen bonds and ionic bonds occur in
the side chains of amino acids in tertiary struc-
Addition of a reducing agent ture.
Placement of the protein in a solution
with a low pH
Increase in the concentration of the pro-
tein in solution
4. An increase in beta-pleated sheet struc- Aggregation of the proteins in the brain
ture in some brain proteins can lead
to an increase in amyloid deposit for- This question is describing changes in pro-
mation, characteristic of some neurode- tein structure. Aggregation occurs when proteins
generative diseases. What is the prima- clump together inappropriately, causing plaques
ry biochemical process that follows the like amyloid deposits to accumulate.
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 exces-
sive ketogenesis
, WGU C785 Biochemistry Unit Exam Questions
Study online at https://quizlet.com/_hseauw
An increase in anaerobic metabolism of
glucose in the brain
5. Which level of protein structure is deter- Primary structure
mined by the sequence of amino acids?
The primary structure of a protein is simply the
Secondary structure sequence of amino acids held together by pep-
tide bonds.
Quaternary structure
Tertiary structure
Primary structure
6. Which force is most influential in de- Hydrogen bonding
termining the secondary structure of a
protein? The secondary structure of a protein is built by
hydrogen bonds between the carboxyl groups
Hydrophobic effect and amino groups on the backbones of the
amino acids.
Disulfide bonding
Hydrogen bonding
Electrostatic interactions
7. Which amino acid would most likely par- Amino Acid structure 4
ticipate 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.
8. Side Chain
, WGU C785 Biochemistry Unit Exam Questions
Study online at https://quizlet.com/_hseauw
Which portion of the amino acid is in- The side chain is the variable group of the
side the box? amino acid, also called the R group. Every amino
acid has the same amino group, carboxylic acid
The box is surrounding the section be- group, and an alpha carbon, but the side chain
low the Alpha Carbon is different.
9. Which pair of amino acids will most like- Both of these amino acids are non-polar and
ly interact through hydrophobic forces therefore can interact together with a hydropho-
between their side chains? bic interaction. Please note that the "S" in the
amino acid on the right is non-polar, while the
"SH" group in answer choice D is polar. The S
must have an H to be polar and is otherwise
non-polar.
10. Which portion of the amino acid is in- Alpha Carbon
side the box?
The alpha carbon is the central carbon on an
The box is over the Carbon at the Center amino acid that holds together the other groups
of the chain of the amino acid. It is always attached to the
amino group, the carboxyl group, the side chain,
and a single hydrogen. It is part of the backbone
of the amino acid and is found in every amino
acid.
11. Given the following amino acid struc- Hydrophobic interaction
ture, what is the strongest intermolec-
ular force it would participate in to sta- The amino acid pictured only has CH groups in its
bilize a protein structure? side chain, and therefore is non-polar. Non-polar
amino acids make hydrophobic interactions.
Ionic bond
Disulfide bond
Study online at https://quizlet.com/_hseauw
1. Which level of protein structure is dis- Primary
rupted through the hydrolysis of pep-
tide bonds? The primary structure of a protein is the se-
quence of amino acids held together by peptide
Quaternary bonds. Peptide bonds are formed by dehydra-
tion reactions and disrupted by hydrolysis.
Tertiary
Primary
Secondary
2. A mutation in the beta-hemoglobin The original amino acid in a healthy patient is
gene, which results in the replacement glutamate, which is negatively charged. The mu-
of the amino acid glutamate in position tated amino acid is valine, which is non-polar. Va-
6 with the amino acid valine, leads to line is causing sickle cell anemia. The best amino
the development of sickle cell anemia. acid to replace valine so that the patient is healthy
The structures of glutamate and valine again would be the one most like glutamate, so
are shown below. any negatively charged amino acid.
If the beta hemoglobin gene in a patient
with sickle-cell anemia were to be edit-
ed 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 out-
come, in theory, for the patient? (As-
sume the valine can potentially be re-
placed with any amino acid other than
glutamate.)
3. Secondary, tertiary, and quaternary lev- Placement of the protein in a solution with a low
els of protein structure can all be im- pH
, WGU C785 Biochemistry Unit Exam Questions
Study online at https://quizlet.com/_hseauw
pacted by exposing a protein to which
treatment? Changes in pH affect hydrogen bonds and ion-
ic bonds. Hydrogen bonds in the backbone of
Change of a hydrophobic amino acid to amino acids occur in secondary structure, and
a different hydrophobic amino acid both hydrogen bonds and ionic bonds occur in
the side chains of amino acids in tertiary struc-
Addition of a reducing agent ture.
Placement of the protein in a solution
with a low pH
Increase in the concentration of the pro-
tein in solution
4. An increase in beta-pleated sheet struc- Aggregation of the proteins in the brain
ture in some brain proteins can lead
to an increase in amyloid deposit for- This question is describing changes in pro-
mation, characteristic of some neurode- tein structure. Aggregation occurs when proteins
generative diseases. What is the prima- clump together inappropriately, causing plaques
ry biochemical process that follows the like amyloid deposits to accumulate.
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 exces-
sive ketogenesis
, WGU C785 Biochemistry Unit Exam Questions
Study online at https://quizlet.com/_hseauw
An increase in anaerobic metabolism of
glucose in the brain
5. Which level of protein structure is deter- Primary structure
mined by the sequence of amino acids?
The primary structure of a protein is simply the
Secondary structure sequence of amino acids held together by pep-
tide bonds.
Quaternary structure
Tertiary structure
Primary structure
6. Which force is most influential in de- Hydrogen bonding
termining the secondary structure of a
protein? The secondary structure of a protein is built by
hydrogen bonds between the carboxyl groups
Hydrophobic effect and amino groups on the backbones of the
amino acids.
Disulfide bonding
Hydrogen bonding
Electrostatic interactions
7. Which amino acid would most likely par- Amino Acid structure 4
ticipate 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.
8. Side Chain
, WGU C785 Biochemistry Unit Exam Questions
Study online at https://quizlet.com/_hseauw
Which portion of the amino acid is in- The side chain is the variable group of the
side the box? amino acid, also called the R group. Every amino
acid has the same amino group, carboxylic acid
The box is surrounding the section be- group, and an alpha carbon, but the side chain
low the Alpha Carbon is different.
9. Which pair of amino acids will most like- Both of these amino acids are non-polar and
ly interact through hydrophobic forces therefore can interact together with a hydropho-
between their side chains? bic interaction. Please note that the "S" in the
amino acid on the right is non-polar, while the
"SH" group in answer choice D is polar. The S
must have an H to be polar and is otherwise
non-polar.
10. Which portion of the amino acid is in- Alpha Carbon
side the box?
The alpha carbon is the central carbon on an
The box is over the Carbon at the Center amino acid that holds together the other groups
of the chain of the amino acid. It is always attached to the
amino group, the carboxyl group, the side chain,
and a single hydrogen. It is part of the backbone
of the amino acid and is found in every amino
acid.
11. Given the following amino acid struc- Hydrophobic interaction
ture, what is the strongest intermolec-
ular force it would participate in to sta- The amino acid pictured only has CH groups in its
bilize a protein structure? side chain, and therefore is non-polar. Non-polar
amino acids make hydrophobic interactions.
Ionic bond
Disulfide bond
