WGU C190 INTRO TO BIOLOGY OA AND
PA 2025/2026 BANK CURRENTLY TESTING
COMPETE 500 QUESTIONS WITH
DETAILED VERIFIED ANSWERS /EXPERT
VERIFIED FOR A+ GUARANTEED /BRAND
NEW!!
Which level of protein structure is disrupted
through the hydrolysis of peptide bonds?
Quaternary
Tertiary
Primary
Secondary – ANSWER 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-haemoglobin 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 anaemia.
The structures of glutamate and valine are shown
below.
If the beta haemoglobin gene in a patient with
sickle-cell anaemia 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.) – ANSWER 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 anaemia. 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 – ANSWER 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 – ANSWER 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
PA 2025/2026 BANK CURRENTLY TESTING
COMPETE 500 QUESTIONS WITH
DETAILED VERIFIED ANSWERS /EXPERT
VERIFIED FOR A+ GUARANTEED /BRAND
NEW!!
Which level of protein structure is disrupted
through the hydrolysis of peptide bonds?
Quaternary
Tertiary
Primary
Secondary – ANSWER 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-haemoglobin 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 anaemia.
The structures of glutamate and valine are shown
below.
If the beta haemoglobin gene in a patient with
sickle-cell anaemia 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.) – ANSWER 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 anaemia. 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 – ANSWER 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 – ANSWER 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
