WGU C785 Biochemistry Unit Exam Questions and
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Terms in this set (67)
Which level of protein structure is disrupted Primary
through the hydrolysis of peptide bonds?
The primary structure of a protein is the sequence of amino
Quaternary acids held together by peptide bonds. Peptide bonds are
formed by dehydration reactions and disrupted by hydrolysis.
Tertiary
Primary
Secondary
A mutation in the beta-hemoglobin gene, The original amino acid in a healthy patient is glutamate, which
which results in the replacement of the is negatively charged. The mutated amino acid is valine,
which amino acid glutamate in position 6 with the is non-polar. Valine is causing sickle cell anemia.
The best amino acid valine, leads to the development amino acid to replace valine so that the
patient is healthy
of sickle cell anemia. The structures of again would be the one most like glutamate, so any
negatively glutamate and valine are shown below. 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.)
,Secondary, tertiary, and quaternary levels of Placement of the protein in a solution with a low pH
protein structure can all be impacted by
exposing a protein to which treatment? Changes in pH affect hydrogen bonds and ionic bonds.
Hydrogen bonds in the backbone of amino acids occur in
Change of a hydrophobic amino acid to a 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
An increase in beta-pleated sheet structure Aggregation of the proteins in the brain
in some brain proteins can lead to an
increase in amyloid deposit formation, This question is describing changes in protein structure.
characteristic of some neurodegenerative Aggregation occurs when proteins clump together
diseases. What is the primary inappropriately, causing plaques like amyloid deposits to
biochemical process that follows the 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 excessive
ketogenesis
An increase in anaerobic metabolism of
glucose in the brain
Which level of protein structure is Primary structure
determined by the sequence of amino
acids? The primary structure of a protein is simply the sequence of
amino acids held together by peptide bonds.
Secondary structure
Quaternary structure
Tertiary structure
Primary structure
, Which force is most influential in Hydrogen bonding
determining the secondary structure of a
protein? The secondary structure of a protein is built by hydrogen
bonds between the carboxyl groups and amino groups on the
Hydrophobic effect backbones of the amino acids.
Disulfide bonding
Hydrogen bonding
Electrostatic interactions
Which amino acid would most likely Amino Acid structure 4
participate 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.
Which portion of the amino acid is inside the Side Chain
box?
The side chain is the variable group of the amino acid, also
The box is surrounding the section below called the R group. Every amino acid has the same amino
the Alpha Carbon group, carboxylic acid group, and an alpha carbon, but the
side chain is different.
Which pair of amino acids will most likely Both of these amino acids are non-polar and therefore can
interact through hydrophobic forces interact together with a hydrophobic interaction. Please note
between their side chains? 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.
Which portion of the amino acid is inside the Alpha Carbon
box?
The alpha carbon is the central carbon on an amino acid that
The box is over the Carbon at the Center of holds together the other groups of the amino acid. It is always
the chain 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.
Given the following amino acid structure, Hydrophobic interaction
what is the strongest intermolecular force it
would participate in to stabilize a protein The amino acid pictured only has CH groups in its side chain,
structure? and therefore is non-polar. Non-polar amino acids make
hydrophobic interactions.
Ionic bond
Disulfide bond
Hydrogen bond
Hydrophobic interaction
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Students also studied
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C
Terms in this set (67)
Which level of protein structure is disrupted Primary
through the hydrolysis of peptide bonds?
The primary structure of a protein is the sequence of amino
Quaternary acids held together by peptide bonds. Peptide bonds are
formed by dehydration reactions and disrupted by hydrolysis.
Tertiary
Primary
Secondary
A mutation in the beta-hemoglobin gene, The original amino acid in a healthy patient is glutamate, which
which results in the replacement of the is negatively charged. The mutated amino acid is valine,
which amino acid glutamate in position 6 with the is non-polar. Valine is causing sickle cell anemia.
The best amino acid valine, leads to the development amino acid to replace valine so that the
patient is healthy
of sickle cell anemia. The structures of again would be the one most like glutamate, so any
negatively glutamate and valine are shown below. 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.)
,Secondary, tertiary, and quaternary levels of Placement of the protein in a solution with a low pH
protein structure can all be impacted by
exposing a protein to which treatment? Changes in pH affect hydrogen bonds and ionic bonds.
Hydrogen bonds in the backbone of amino acids occur in
Change of a hydrophobic amino acid to a 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
An increase in beta-pleated sheet structure Aggregation of the proteins in the brain
in some brain proteins can lead to an
increase in amyloid deposit formation, This question is describing changes in protein structure.
characteristic of some neurodegenerative Aggregation occurs when proteins clump together
diseases. What is the primary inappropriately, causing plaques like amyloid deposits to
biochemical process that follows the 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 excessive
ketogenesis
An increase in anaerobic metabolism of
glucose in the brain
Which level of protein structure is Primary structure
determined by the sequence of amino
acids? The primary structure of a protein is simply the sequence of
amino acids held together by peptide bonds.
Secondary structure
Quaternary structure
Tertiary structure
Primary structure
, Which force is most influential in Hydrogen bonding
determining the secondary structure of a
protein? The secondary structure of a protein is built by hydrogen
bonds between the carboxyl groups and amino groups on the
Hydrophobic effect backbones of the amino acids.
Disulfide bonding
Hydrogen bonding
Electrostatic interactions
Which amino acid would most likely Amino Acid structure 4
participate 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.
Which portion of the amino acid is inside the Side Chain
box?
The side chain is the variable group of the amino acid, also
The box is surrounding the section below called the R group. Every amino acid has the same amino
the Alpha Carbon group, carboxylic acid group, and an alpha carbon, but the
side chain is different.
Which pair of amino acids will most likely Both of these amino acids are non-polar and therefore can
interact through hydrophobic forces interact together with a hydrophobic interaction. Please note
between their side chains? 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.
Which portion of the amino acid is inside the Alpha Carbon
box?
The alpha carbon is the central carbon on an amino acid that
The box is over the Carbon at the Center of holds together the other groups of the amino acid. It is always
the chain 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.
Given the following amino acid structure, Hydrophobic interaction
what is the strongest intermolecular force it
would participate in to stabilize a protein The amino acid pictured only has CH groups in its side chain,
structure? and therefore is non-polar. Non-polar amino acids make
hydrophobic interactions.
Ionic bond
Disulfide bond
Hydrogen bond
Hydrophobic interaction
