WGU C785 LATEST 2026 EXAM QUESTIONS AND
ANSWERS RATED A+
✔✔Neurodegenerative protein aggregation - ✔✔Alzheimer's disease, the most common
neurodegenerative disease. The formation of aggregated amyloid-beta fibers is another
characteristic of Alzheimer's disease, but neurodegeneration and memory loss can be
detected before amyloid fibers accumulate in the brain.
✔✔molecular chaperones - ✔✔A protein that helps other proteins fold or refold from a
partially denatured state.
✔✔Primary level of protein structure - ✔✔chain of amino acids, peptide bonds forming a
polypeptide chain. Covalent bond, does not denature
✔✔Secondary level of protein structure - ✔✔alpha helix (coil) and beta-pleated sheet,
hydrogen bond, denatured by salt and Ph change, contain carboxyl and amino groups
✔✔Tertiary level of protein structure - ✔✔side chain interaction, (R-group) - (3D), ex.
sickle cell, arthritis, hemophilia. Changes seen with increased temp, salt, change in pH
and reducing agents.
✔✔Quaternary subunit - ✔✔more than one polypeptide, Ex: Hemoglobin. Changes
seen with increased temp.
✔✔Primary formed by - ✔✔peptide bonds
✔✔Secondary formed by - ✔✔held together by hydrogen bonds which are formed by 2
polar amino acids
✔✔Which structure is unaffected by complete denaturation of the multi-subunit -
✔✔Primary - peptide bonds are strong and covalent located in backbone and does not
denature
✔✔Tertiary structure is hydrophobic - ✔✔Protein structure is stabilized primarily by the
hydrophobic effect; disruption of the hydrophobic effect is the simplest way to denature
a protein this is done by heating it up.
✔✔What does the alpha and beta sheets make up? - ✔✔Secondary structure
✔✔Methotrexate - ✔✔works by blocking an enzyme process in cancer cells so they can
not grow
✔✔APC - ✔✔gene decreased expression because of methyl group. APC is classified as
tumor suppressor gene.
, ✔✔induced fit - ✔✔The substrate and active site are somewhat complementary prior to
substrate binding, many enzymes will adjust their active site conformation slightly as the
substrate binds to improve the fit.
✔✔Substrate enzyme complex - like a lock and key - ✔✔Each substrate binds to an
active site, producing an enzyme-substrate complex. The geometric and the chemical
complementarity between the enzyme and substrate depend on noncovalent forces.
✔✔Substrate - ✔✔A specific reactant acted upon by an enzyme, Enzymes have an
active site, which serves as the binding platform for its specific substrate(s) and acts as
the site of the chemical reaction
✔✔Enzyme inhibition ( competitive vs non competitive)
A competitive inhibitor - ✔✔is usually a molecule similar in structure to a substrate that
can bind to an enzyme's active site even though the molecule is unable to react
✔✔Noncompetitive inhibitors - ✔✔Some noncompetitive inhibitors attach to the enzyme
at an allosteric site, which is a site other than the active site
✔✔• Feedback inhibition (non-competitive) - KNOW WHAT PICTURES OF INHIBITION
LOOK LIKE AND RECOGNIZE STRUCTURES - ✔✔once end product builds up it will
bind to the allosteric site on the first enzyme and stop the pathway! - it binds to the
enzyme slowing the product.
✔✔Amino acids - what makes it non-polar - ✔✔Contains carbons and Hydrogens (CH,
CH2, CH3)-Weak interactions that tend to go in the middle of the protein (aggregation)
affected by temp change.
✔✔What part of the phospholipid is hydrophobic - ✔✔The tails
✔✔Peptide bond - ✔✔form between two amino acids via a dehydration reaction. During
the reaction, a water molecule (H2O) forms from the oxygen of a carboxyl group and
two hydrogens from an amino group. As water forms, the carbon atom of the carboxyl
group and the nitrogen atom of the amino group become bonded together. This bond
between the two amino acids is called a peptide bond.
✔✔cooperative bonding on hemoglobin - ✔✔The four subunits of hemoglobin work
together. When one molecule of oxygen leaves the other three tend to leave too. When
one picks up oxygen the others tend to pick it up to. This is how it is picked up in the
lungs and dropped off in the tissues.
✔✔Cooperative binding - ✔✔O2 will bind quicker to hemoglobin if there is another O2
molecule already binding
ANSWERS RATED A+
✔✔Neurodegenerative protein aggregation - ✔✔Alzheimer's disease, the most common
neurodegenerative disease. The formation of aggregated amyloid-beta fibers is another
characteristic of Alzheimer's disease, but neurodegeneration and memory loss can be
detected before amyloid fibers accumulate in the brain.
✔✔molecular chaperones - ✔✔A protein that helps other proteins fold or refold from a
partially denatured state.
✔✔Primary level of protein structure - ✔✔chain of amino acids, peptide bonds forming a
polypeptide chain. Covalent bond, does not denature
✔✔Secondary level of protein structure - ✔✔alpha helix (coil) and beta-pleated sheet,
hydrogen bond, denatured by salt and Ph change, contain carboxyl and amino groups
✔✔Tertiary level of protein structure - ✔✔side chain interaction, (R-group) - (3D), ex.
sickle cell, arthritis, hemophilia. Changes seen with increased temp, salt, change in pH
and reducing agents.
✔✔Quaternary subunit - ✔✔more than one polypeptide, Ex: Hemoglobin. Changes
seen with increased temp.
✔✔Primary formed by - ✔✔peptide bonds
✔✔Secondary formed by - ✔✔held together by hydrogen bonds which are formed by 2
polar amino acids
✔✔Which structure is unaffected by complete denaturation of the multi-subunit -
✔✔Primary - peptide bonds are strong and covalent located in backbone and does not
denature
✔✔Tertiary structure is hydrophobic - ✔✔Protein structure is stabilized primarily by the
hydrophobic effect; disruption of the hydrophobic effect is the simplest way to denature
a protein this is done by heating it up.
✔✔What does the alpha and beta sheets make up? - ✔✔Secondary structure
✔✔Methotrexate - ✔✔works by blocking an enzyme process in cancer cells so they can
not grow
✔✔APC - ✔✔gene decreased expression because of methyl group. APC is classified as
tumor suppressor gene.
, ✔✔induced fit - ✔✔The substrate and active site are somewhat complementary prior to
substrate binding, many enzymes will adjust their active site conformation slightly as the
substrate binds to improve the fit.
✔✔Substrate enzyme complex - like a lock and key - ✔✔Each substrate binds to an
active site, producing an enzyme-substrate complex. The geometric and the chemical
complementarity between the enzyme and substrate depend on noncovalent forces.
✔✔Substrate - ✔✔A specific reactant acted upon by an enzyme, Enzymes have an
active site, which serves as the binding platform for its specific substrate(s) and acts as
the site of the chemical reaction
✔✔Enzyme inhibition ( competitive vs non competitive)
A competitive inhibitor - ✔✔is usually a molecule similar in structure to a substrate that
can bind to an enzyme's active site even though the molecule is unable to react
✔✔Noncompetitive inhibitors - ✔✔Some noncompetitive inhibitors attach to the enzyme
at an allosteric site, which is a site other than the active site
✔✔• Feedback inhibition (non-competitive) - KNOW WHAT PICTURES OF INHIBITION
LOOK LIKE AND RECOGNIZE STRUCTURES - ✔✔once end product builds up it will
bind to the allosteric site on the first enzyme and stop the pathway! - it binds to the
enzyme slowing the product.
✔✔Amino acids - what makes it non-polar - ✔✔Contains carbons and Hydrogens (CH,
CH2, CH3)-Weak interactions that tend to go in the middle of the protein (aggregation)
affected by temp change.
✔✔What part of the phospholipid is hydrophobic - ✔✔The tails
✔✔Peptide bond - ✔✔form between two amino acids via a dehydration reaction. During
the reaction, a water molecule (H2O) forms from the oxygen of a carboxyl group and
two hydrogens from an amino group. As water forms, the carbon atom of the carboxyl
group and the nitrogen atom of the amino group become bonded together. This bond
between the two amino acids is called a peptide bond.
✔✔cooperative bonding on hemoglobin - ✔✔The four subunits of hemoglobin work
together. When one molecule of oxygen leaves the other three tend to leave too. When
one picks up oxygen the others tend to pick it up to. This is how it is picked up in the
lungs and dropped off in the tissues.
✔✔Cooperative binding - ✔✔O2 will bind quicker to hemoglobin if there is another O2
molecule already binding
