1
WGU C785 BIOCHEMISTRY OA
FINAL EXAM
GUARANTEED PASS ON 1ST ATTEMPT
Which level of protein Primary
structure is disrupted
through the The primary structure of a protein is the
hydrolysis of sequence of amino acids held together by
peptide bonds. Peptide bonds are formed
peptide bonds? by dehydration reactions and disrupted by
hydrolysis.
Quaternary
Tertiary
Primary
Secondary
,2
A mutation in the The original amino acid in a healthy patient is
beta- hemoglobin glutamate, which is negatively charged. The
gene, which results in mutated amino acid is valine, which is non-
the replacement of the polar. Valine is causing sickle cell anemia.
amino acid glutamate The best amino acid to replace valine so
in position 6 with the that the patient is healthy again would be
amino acid valine, the one most like glutamate, so any negatively
leads to the charged amino acid.
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
expected to have the
best clinical outcome,
in theory, for the
patient? (Assume
,3
the valine can
potentially be
replaced with any
amino acid
other than glutamate.)
Secondary, tertiary, Placement of the protein in a solution with a low pH
and quaternary levels
of protein Changes in pH affect hydrogen bonds and ionic
bonds.
structure can all be
Hydrogen bonds in the backbone of amino acids
impacted by exposing a occur in
protein to which secondary structure, and both hydrogen
treatment?
bonds and ionic bonds occur in the side
chains of amino acids in tertiary structure.
Change of a
hydrophobic amino
acid to a different
hydrophobic amino
acid
Addition of a reducing
agent
, 4
Placement of the
protein in a solution
with a low pH
Increase in the
concentration of the
protein in solution
WGU C785 BIOCHEMISTRY OA
FINAL EXAM
GUARANTEED PASS ON 1ST ATTEMPT
Which level of protein Primary
structure is disrupted
through the The primary structure of a protein is the
hydrolysis of sequence of amino acids held together by
peptide bonds. Peptide bonds are formed
peptide bonds? by dehydration reactions and disrupted by
hydrolysis.
Quaternary
Tertiary
Primary
Secondary
,2
A mutation in the The original amino acid in a healthy patient is
beta- hemoglobin glutamate, which is negatively charged. The
gene, which results in mutated amino acid is valine, which is non-
the replacement of the polar. Valine is causing sickle cell anemia.
amino acid glutamate The best amino acid to replace valine so
in position 6 with the that the patient is healthy again would be
amino acid valine, the one most like glutamate, so any negatively
leads to the charged amino acid.
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
expected to have the
best clinical outcome,
in theory, for the
patient? (Assume
,3
the valine can
potentially be
replaced with any
amino acid
other than glutamate.)
Secondary, tertiary, Placement of the protein in a solution with a low pH
and quaternary levels
of protein Changes in pH affect hydrogen bonds and ionic
bonds.
structure can all be
Hydrogen bonds in the backbone of amino acids
impacted by exposing a occur in
protein to which secondary structure, and both hydrogen
treatment?
bonds and ionic bonds occur in the side
chains of amino acids in tertiary structure.
Change of a
hydrophobic amino
acid to a different
hydrophobic amino
acid
Addition of a reducing
agent
, 4
Placement of the
protein in a solution
with a low pH
Increase in the
concentration of the
protein in solution
