WGU C785 Biochemistry Unit Questions with|\ |\ |\ |\ |\ |\
answers
Which level of protein structure is disrupted through the
|\ |\ |\ |\ |\ |\ |\ |\ |\
hydrolysis of peptide bonds? |\ |\ |\
Quaternary
Tertiary
Primary
Secondary - CORRECT ANSWERS ✔✔Primary |\ |\ |\ |\
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 by hydrolysis. |\ |\ |\ |\ |\
A mutation in the beta-hemoglobin gene, which results in the
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
replacement of the amino acid glutamate in position 6 with the |\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
amino acid valine, leads to the 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 the valine can potentially be replaced with any
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
amino acid other than glutamate.) - CORRECT ANSWERS ✔✔The
|\ |\ |\ |\ |\ |\ |\ |\ |\
original amino acid in a healthy patient is glutamate, which is
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
negatively charged. The mutated amino acid is valine, which is
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
non-polar. Valine is causing sickle cell anemia. The best amino
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
acid to replace valine so that the patient is healthy again would
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
be the one most like glutamate, so any negatively charged amino
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
acid.
|\
Secondary, tertiary, and quaternary levels of protein structure
|\ |\ |\ |\ |\ |\ |\ |\
can all be impacted by exposing a protein to which treatment?
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
Change of a hydrophobic amino acid to a different hydrophobic
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
amino acid |\
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 ANSWERS ✔✔Placement of the protein in a solution
|\ |\ |\ |\ |\ |\ |\ |\ |\
with a low pH |\ |\ |\
Changes in pH affect hydrogen bonds and ionic bonds. Hydrogen
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
bonds in the backbone of amino acids occur in secondary
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
structure, and both hydrogen bonds and ionic bonds occur in the
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
side chains of amino acids in tertiary structure.
|\ |\ |\ |\ |\ |\ |\
,An increase in beta-pleated sheet structure in some brain
|\ |\ |\ |\ |\ |\ |\ |\ |\
proteins can lead to an increase in amyloid deposit formation,
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
characteristic of some neurodegenerative diseases. What is the
|\ |\ |\ |\ |\ |\ |\ |\
primary biochemical 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 -
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
CORRECT ANSWERS ✔✔Aggregation of the proteins in the brain
|\ |\ |\ |\ |\ |\ |\ |\
This question is describing changes in protein structure.
|\ |\ |\ |\ |\ |\ |\ |\
Aggregation occurs when proteins clump together |\ |\ |\ |\ |\ |\
inappropriately, causing plaques like amyloid deposits to |\ |\ |\ |\ |\ |\ |\
accumulate.
Which level of protein structure is determined by the sequence of
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
amino acids?
|\ |\
Secondary structure |\
Quaternary structure |\
, Tertiary structure
|\
Primary structure - CORRECT ANSWERS ✔✔Primary structure
|\ |\ |\ |\ |\ |\
The primary structure of a protein is simply the sequence of
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
amino acids held together by peptide bonds.
|\ |\ |\ |\ |\ |\
Which force is most influential in determining the secondary
|\ |\ |\ |\ |\ |\ |\ |\ |\
structure of a protein? |\ |\ |\
Hydrophobic effect |\
Disulfide bonding |\
Hydrogen bonding |\
Electrostatic interactions - CORRECT ANSWERS ✔✔Hydrogen
|\ |\ |\ |\ |\ |\
bonding
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. |\ |\ |\ |\
Which amino acid would most likely participate in hydrogen
|\ |\ |\ |\ |\ |\ |\ |\ |\
bonds? - CORRECT ANSWERS ✔✔Amino Acid structure 4
|\ |\ |\ |\ |\ |\ |\
answers
Which level of protein structure is disrupted through the
|\ |\ |\ |\ |\ |\ |\ |\ |\
hydrolysis of peptide bonds? |\ |\ |\
Quaternary
Tertiary
Primary
Secondary - CORRECT ANSWERS ✔✔Primary |\ |\ |\ |\
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 by hydrolysis. |\ |\ |\ |\ |\
A mutation in the beta-hemoglobin gene, which results in the
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
replacement of the amino acid glutamate in position 6 with the |\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
amino acid valine, leads to the 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 the valine can potentially be replaced with any
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
amino acid other than glutamate.) - CORRECT ANSWERS ✔✔The
|\ |\ |\ |\ |\ |\ |\ |\ |\
original amino acid in a healthy patient is glutamate, which is
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
negatively charged. The mutated amino acid is valine, which is
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
non-polar. Valine is causing sickle cell anemia. The best amino
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
acid to replace valine so that the patient is healthy again would
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
be the one most like glutamate, so any negatively charged amino
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
acid.
|\
Secondary, tertiary, and quaternary levels of protein structure
|\ |\ |\ |\ |\ |\ |\ |\
can all be impacted by exposing a protein to which treatment?
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
Change of a hydrophobic amino acid to a different hydrophobic
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
amino acid |\
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 ANSWERS ✔✔Placement of the protein in a solution
|\ |\ |\ |\ |\ |\ |\ |\ |\
with a low pH |\ |\ |\
Changes in pH affect hydrogen bonds and ionic bonds. Hydrogen
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
bonds in the backbone of amino acids occur in secondary
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
structure, and both hydrogen bonds and ionic bonds occur in the
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
side chains of amino acids in tertiary structure.
|\ |\ |\ |\ |\ |\ |\
,An increase in beta-pleated sheet structure in some brain
|\ |\ |\ |\ |\ |\ |\ |\ |\
proteins can lead to an increase in amyloid deposit formation,
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
characteristic of some neurodegenerative diseases. What is the
|\ |\ |\ |\ |\ |\ |\ |\
primary biochemical 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 -
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
CORRECT ANSWERS ✔✔Aggregation of the proteins in the brain
|\ |\ |\ |\ |\ |\ |\ |\
This question is describing changes in protein structure.
|\ |\ |\ |\ |\ |\ |\ |\
Aggregation occurs when proteins clump together |\ |\ |\ |\ |\ |\
inappropriately, causing plaques like amyloid deposits to |\ |\ |\ |\ |\ |\ |\
accumulate.
Which level of protein structure is determined by the sequence of
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\
amino acids?
|\ |\
Secondary structure |\
Quaternary structure |\
, Tertiary structure
|\
Primary structure - CORRECT ANSWERS ✔✔Primary structure
|\ |\ |\ |\ |\ |\
The primary structure of a protein is simply the sequence of
|\ |\ |\ |\ |\ |\ |\ |\ |\ |\ |\
amino acids held together by peptide bonds.
|\ |\ |\ |\ |\ |\
Which force is most influential in determining the secondary
|\ |\ |\ |\ |\ |\ |\ |\ |\
structure of a protein? |\ |\ |\
Hydrophobic effect |\
Disulfide bonding |\
Hydrogen bonding |\
Electrostatic interactions - CORRECT ANSWERS ✔✔Hydrogen
|\ |\ |\ |\ |\ |\
bonding
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. |\ |\ |\ |\
Which amino acid would most likely participate in hydrogen
|\ |\ |\ |\ |\ |\ |\ |\ |\
bonds? - CORRECT ANSWERS ✔✔Amino Acid structure 4
|\ |\ |\ |\ |\ |\ |\
