WGU C785 Final Exam with all solution
correct answer
A mutation in the beta-hemoglobin gene,
which results in the replacement of the The original amino acid in a healthy patient is glutamate,
amino acid glutamate in position 6 with the which is negatively charged. The mutated amino acid is
amino acid valine, leads to the development valine, which is non-polar. Valine is causing sickle cell
of sickle cell anemia. The structures of anemia. The best amino acid to replace valine so that the
glutamate and valine are shown below. patient is healthy again would be the one most like
glutamate, so any negatively charged amino acid.
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.)
correct answer
Secondary, tertiary, and quaternary levels of
protein structure can all be impacted by Placement of the protein in a solution with a low pH
exposing a protein to which treatment?
Changes in pH affect hydrogen bonds and ionic bonds.
Change of a hydrophobic amino acid to a Hydrogen bonds in the backbone of amino acids occur in
secondary structure, and both hydrogen bonds and ionic
different hydrophobic amino acid
bonds occur in the side chains of amino acids in tertiary
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
correct answer
An increase in beta-pleated sheet structure
in some brain proteins can lead to an Aggregation of the proteins in the brain
increase in amyloid deposit formation,
characteristic of some neurodegenerative This question is describing changes in protein structure.
diseases. What is the primary Aggregation occurs when proteins clump together
biochemical process that follows the inappropriately, causing plaques like amyloid deposits to
increase in beta-pleated sheet structure accumulate.
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
correct answer
A mutation in the beta-hemoglobin gene,
which results in the replacement of the The original amino acid in a healthy patient is glutamate,
amino acid glutamate in position 6 with the which is negatively charged. The mutated amino acid is
amino acid valine, leads to the development valine, which is non-polar. Valine is causing sickle cell
of sickle cell anemia. The structures of anemia. The best amino acid to replace valine so that the
glutamate and valine are shown below. patient is healthy again would be the one most like
glutamate, so any negatively charged amino acid.
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.)
correct answer
Secondary, tertiary, and quaternary levels of
protein structure can all be impacted by Placement of the protein in a solution with a low pH
exposing a protein to which treatment?
Changes in pH affect hydrogen bonds and ionic bonds.
Change of a hydrophobic amino acid to a Hydrogen bonds in the backbone of amino acids occur in
secondary structure, and both hydrogen bonds and ionic
different hydrophobic amino acid
bonds occur in the side chains of amino acids in tertiary
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
correct answer
An increase in beta-pleated sheet structure
in some brain proteins can lead to an Aggregation of the proteins in the brain
increase in amyloid deposit formation,
characteristic of some neurodegenerative This question is describing changes in protein structure.
diseases. What is the primary Aggregation occurs when proteins clump together
biochemical process that follows the inappropriately, causing plaques like amyloid deposits to
increase in beta-pleated sheet structure accumulate.
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
