BIOCHEM C785 FINAL PAPER TESTED
QUESTIONS AND ANSWERS 2026.
◍ 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.). 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 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. 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
Tertiary structure
Primary structure. Answer: 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. Answer: 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?. Answer: Amino Acid structure 4
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 box?
The box is surrounding the section below the Alpha Carbon. Answer:
Side Chain
The side chain is the variable group of the amino acid, also called the
R group. Every amino acid has the same amino group, carboxylic acid
group, and an alpha carbon, but the side chain is different.
QUESTIONS AND ANSWERS 2026.
◍ 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.). 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 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. 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
Tertiary structure
Primary structure. Answer: 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. Answer: 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?. Answer: Amino Acid structure 4
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 box?
The box is surrounding the section below the Alpha Carbon. Answer:
Side Chain
The side chain is the variable group of the amino acid, also called the
R group. Every amino acid has the same amino group, carboxylic acid
group, and an alpha carbon, but the side chain is different.
