WGU 785 FINAL EXAM LATEST 2026/2026
WITH COMPLETE SOLUTION100%
CORRECT |GRADED A +
subunit - ANSWER Each polypeptide chain that is part of a larger protein
hydrophobic effect - ANSWER Hydrophobic R groups cluster together in the
interior of a protein to minimize their contact with water. (This stabilizes the folded
polypeptide backbone) induces aggregation
hydrophobic interactions - ANSWER Slight attraction (very weak) when non-
polar groups are close together and result in hydrophobic protein core and
hydrophilic proteins on the surface ( globular or spherical proteins- i.e.,
hemoglobin)
hydrogen bond - ANSWER Bonds between a hydrogen atom and oxygen atom
of another amino acid side chain ( between non-polar amino acids, ends in C-H's)
Ionic bond - ANSWER Forms between 2 oppositely charged side chains of the
charged amino acids ( AKA salt bridge or ion pair)
Disulfide bond - ANSWER 2 cysteine R groups come together to form a
covalent disulfide bond between the 2 sulfur atoms
, Polar bond - ANSWER a covalent bond in which electrons are shared unequally
( ends in OH, NH, SH, or H)
aggregate - ANSWER Hydrophobic molecules clump together in a disorderly
way
Chaperones - ANSWER Helper molecules that assist in the protein folding of a
newly made polypeptide
Degradation - ANSWER Protein is broken down back into individual amino
acids and recycled into other proteins.
Denaturation - ANSWER loss of normal shape of a protein due to
heat(hydrophobic interactions) , changes in pH(ionic/hydrogen bonds), high salt
concentrations( ionic/hydrogen bonds) or reducing agents ( disulfide bonds)
catalyst - ANSWER substance that speeds up the rate of a chemical reaction
and remains unchanged from the reaction ( this is what enzymes are)
activation energy - ANSWER Energy needed to get a reaction started
Substrate - ANSWER A specific molecule on which an enzyme works.
active site - ANSWER The binding platform part of an enzyme for its specific
substrate.
,Substrate bonding affinity - ANSWER Attraction of substrate to the active site
of an enzyme
phosphorylation - ANSWER Kinase- Attachment of a phosphate group of a
polar amino acid to modify a protein to regulate enzyme activity
Dephosphorylation - ANSWER Phosphatases- Removal of a phosphate group
of a polar amino acid to modify a protein to regulate enzyme activity
Allosteric site - ANSWER A site on an enzyme other than the active site to
which noncompetitive inhibitors bind, changing the shape and activity of the
enzyme.
Feedback inhibition - ANSWER A kind of reversible non-competitive inhibitor
that regulates the rate and affects many metabolic pathways ( when the final
product has built up enough, it signals an enzyme in the front of the cycle to cease
the reaction)
Competitive inhibitor - ANSWER Molecule that competes with substrate to
bind to the active site
Induced fit - ANSWER Active site conforms slightly to better accommodate the
substrate ( hugs the substrate)
what is a beta linkage? - ANSWER seen in plant polysaccharides. Face in
opposite directions.
, what is insulin? - ANSWER hormone; lowers blood sugar
what is glucagon? - ANSWER hormone; raises blood sugar
what is glycogen? - ANSWER form of glucose storage in the liver
What is glycogenesis? - ANSWER formation of glycogen from glucose
what is glut4? - ANSWER glucose transporter
what is glycogenolysis? - ANSWER glycogen breakdown, release of glucose
What is aerobic metabolism? - ANSWER ATP production using oxygen breaks
down fats and carbs.
What is cellular respiration? - ANSWER cathbolic pathways of aerobic and
anaerobic; break down molecules by using the electron transport chain for ATP
production
what is glycolysis? - ANSWER breakdown of glucose, creates 2 new ATP and 2
pyruvate
What is the citric acid cycle? - ANSWER creation of 3 NADH and 1 FADH2
and 2 CO2 molecules in each turn of the cycle
WITH COMPLETE SOLUTION100%
CORRECT |GRADED A +
subunit - ANSWER Each polypeptide chain that is part of a larger protein
hydrophobic effect - ANSWER Hydrophobic R groups cluster together in the
interior of a protein to minimize their contact with water. (This stabilizes the folded
polypeptide backbone) induces aggregation
hydrophobic interactions - ANSWER Slight attraction (very weak) when non-
polar groups are close together and result in hydrophobic protein core and
hydrophilic proteins on the surface ( globular or spherical proteins- i.e.,
hemoglobin)
hydrogen bond - ANSWER Bonds between a hydrogen atom and oxygen atom
of another amino acid side chain ( between non-polar amino acids, ends in C-H's)
Ionic bond - ANSWER Forms between 2 oppositely charged side chains of the
charged amino acids ( AKA salt bridge or ion pair)
Disulfide bond - ANSWER 2 cysteine R groups come together to form a
covalent disulfide bond between the 2 sulfur atoms
, Polar bond - ANSWER a covalent bond in which electrons are shared unequally
( ends in OH, NH, SH, or H)
aggregate - ANSWER Hydrophobic molecules clump together in a disorderly
way
Chaperones - ANSWER Helper molecules that assist in the protein folding of a
newly made polypeptide
Degradation - ANSWER Protein is broken down back into individual amino
acids and recycled into other proteins.
Denaturation - ANSWER loss of normal shape of a protein due to
heat(hydrophobic interactions) , changes in pH(ionic/hydrogen bonds), high salt
concentrations( ionic/hydrogen bonds) or reducing agents ( disulfide bonds)
catalyst - ANSWER substance that speeds up the rate of a chemical reaction
and remains unchanged from the reaction ( this is what enzymes are)
activation energy - ANSWER Energy needed to get a reaction started
Substrate - ANSWER A specific molecule on which an enzyme works.
active site - ANSWER The binding platform part of an enzyme for its specific
substrate.
,Substrate bonding affinity - ANSWER Attraction of substrate to the active site
of an enzyme
phosphorylation - ANSWER Kinase- Attachment of a phosphate group of a
polar amino acid to modify a protein to regulate enzyme activity
Dephosphorylation - ANSWER Phosphatases- Removal of a phosphate group
of a polar amino acid to modify a protein to regulate enzyme activity
Allosteric site - ANSWER A site on an enzyme other than the active site to
which noncompetitive inhibitors bind, changing the shape and activity of the
enzyme.
Feedback inhibition - ANSWER A kind of reversible non-competitive inhibitor
that regulates the rate and affects many metabolic pathways ( when the final
product has built up enough, it signals an enzyme in the front of the cycle to cease
the reaction)
Competitive inhibitor - ANSWER Molecule that competes with substrate to
bind to the active site
Induced fit - ANSWER Active site conforms slightly to better accommodate the
substrate ( hugs the substrate)
what is a beta linkage? - ANSWER seen in plant polysaccharides. Face in
opposite directions.
, what is insulin? - ANSWER hormone; lowers blood sugar
what is glucagon? - ANSWER hormone; raises blood sugar
what is glycogen? - ANSWER form of glucose storage in the liver
What is glycogenesis? - ANSWER formation of glycogen from glucose
what is glut4? - ANSWER glucose transporter
what is glycogenolysis? - ANSWER glycogen breakdown, release of glucose
What is aerobic metabolism? - ANSWER ATP production using oxygen breaks
down fats and carbs.
What is cellular respiration? - ANSWER cathbolic pathways of aerobic and
anaerobic; break down molecules by using the electron transport chain for ATP
production
what is glycolysis? - ANSWER breakdown of glucose, creates 2 new ATP and 2
pyruvate
What is the citric acid cycle? - ANSWER creation of 3 NADH and 1 FADH2
and 2 CO2 molecules in each turn of the cycle
