WGU C785 LATEST 2026 TEST PAPER QUESTIONS AND
ANSWERS RATED A+
✔✔• 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
✔✔CO (carbon monoxide) binding with hemoglobin - pick up - ✔✔CO binds to the same
group as O2 but it binds more strongly. If CO is there it will pick up the O2 but it won't
drop it off. This is why CO positioning is so harmful. The pt. is usually very pink in color.
CO stabilizes the R-state by CO binding to the same FE in Hgb and changes the heme
shape.
✔✔2,3 BPG and O2 affinity for fetus - ✔✔Affinity= stickiness for 02, a human fetus
needs a higher affinity for oxygen to get it from its mother. The mother 2,3 BPG is
higher so their affinity for oxygen is lower. The mom becomes deoxygenated.
✔✔how is hemoglobin structure is affected in the absence of 02 - ✔✔This is found in
the muscles. The structure is tense, heme is domed shaped and ph is lower.
✔✔hemoglobin - ✔✔low affinity for O2 and transports it throughout the body
✔✔myoglobin - ✔✔has a high affinity for O2 and stores it. Not affected by change in pH
, ✔✔How pH influences O2 saturation of hemoglobin at the same partial pressure. -
✔✔pH was 7.2 and 7.4 and pressure was 90 torr - Left shift = increased affinity for O2
Right shift = decreased affinity for O2
The same torr but a 7.2 going to 7.4; higher PH would mean it would have an increased
in affinity for O2; increased in hemoglobin saturation; reach 100% earlier
✔✔(Bohr effect): Ph is the signal for hemoglobin to let go of O2 - ✔✔CHART
C: Increase Co2
H: Increase in H
A: Acidic
R: Release O2
T: Tense Tissues
✔✔What makes LDL - ✔✔high cholesterol - Made of a 4 ring structure. AKA sterols
(cholesterol, cortisol and testosterone). It expands range of membernes fluid; greatest
membrane fluidity. It increases the temp to solidify.
✔✔Cholesterol is needed to synthesize - ✔✔vitamin D in the skin; cholic acid, a
component of bile; and steroid hormones.
✔✔steroid hormones - ✔✔include testosterone and estrogen, which promote growth
and the development of sex characteristics,
✔✔cortisol - ✔✔which is released in response to stress and promotes glucose synthesis
in the liver
✔✔myoglobin - ✔✔protein with a single subunit containing heme and iron. Normally
contained only in the muscles, it can be released into the bloodstream if there is muscle
damage. For this reason, measuring the levels of myoglobin in the blood can provide
evidence of rhabdomyolysis, a mild heart attack, or a muscular degenerative disease.
✔✔Anabolic pathway - ✔✔Anabolic pathways are those that require energy to
synthesize larger molecules. This is when there is no O2 the ETC can not work. When
NAD+ runs out it makes it with fermentation lactate regenerates the NADH to NAD+ that
was used during glycolysis to make small amounts of ATP and lactate
✔✔Cori Cycle - ✔✔uses the lactate made by fermentation in the liver and uses
gluconeogenesis to covert two lactate to glucose. 2 ATP are made with each cycle but it
uses 6. So the net loss is -4 ATP>
✔✔catabolic pathway - ✔✔those that generate energy by breaking down larger
molecules. Both types of pathways are required for maintaining the cell's energy
balance
ANSWERS RATED A+
✔✔• 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
✔✔CO (carbon monoxide) binding with hemoglobin - pick up - ✔✔CO binds to the same
group as O2 but it binds more strongly. If CO is there it will pick up the O2 but it won't
drop it off. This is why CO positioning is so harmful. The pt. is usually very pink in color.
CO stabilizes the R-state by CO binding to the same FE in Hgb and changes the heme
shape.
✔✔2,3 BPG and O2 affinity for fetus - ✔✔Affinity= stickiness for 02, a human fetus
needs a higher affinity for oxygen to get it from its mother. The mother 2,3 BPG is
higher so their affinity for oxygen is lower. The mom becomes deoxygenated.
✔✔how is hemoglobin structure is affected in the absence of 02 - ✔✔This is found in
the muscles. The structure is tense, heme is domed shaped and ph is lower.
✔✔hemoglobin - ✔✔low affinity for O2 and transports it throughout the body
✔✔myoglobin - ✔✔has a high affinity for O2 and stores it. Not affected by change in pH
, ✔✔How pH influences O2 saturation of hemoglobin at the same partial pressure. -
✔✔pH was 7.2 and 7.4 and pressure was 90 torr - Left shift = increased affinity for O2
Right shift = decreased affinity for O2
The same torr but a 7.2 going to 7.4; higher PH would mean it would have an increased
in affinity for O2; increased in hemoglobin saturation; reach 100% earlier
✔✔(Bohr effect): Ph is the signal for hemoglobin to let go of O2 - ✔✔CHART
C: Increase Co2
H: Increase in H
A: Acidic
R: Release O2
T: Tense Tissues
✔✔What makes LDL - ✔✔high cholesterol - Made of a 4 ring structure. AKA sterols
(cholesterol, cortisol and testosterone). It expands range of membernes fluid; greatest
membrane fluidity. It increases the temp to solidify.
✔✔Cholesterol is needed to synthesize - ✔✔vitamin D in the skin; cholic acid, a
component of bile; and steroid hormones.
✔✔steroid hormones - ✔✔include testosterone and estrogen, which promote growth
and the development of sex characteristics,
✔✔cortisol - ✔✔which is released in response to stress and promotes glucose synthesis
in the liver
✔✔myoglobin - ✔✔protein with a single subunit containing heme and iron. Normally
contained only in the muscles, it can be released into the bloodstream if there is muscle
damage. For this reason, measuring the levels of myoglobin in the blood can provide
evidence of rhabdomyolysis, a mild heart attack, or a muscular degenerative disease.
✔✔Anabolic pathway - ✔✔Anabolic pathways are those that require energy to
synthesize larger molecules. This is when there is no O2 the ETC can not work. When
NAD+ runs out it makes it with fermentation lactate regenerates the NADH to NAD+ that
was used during glycolysis to make small amounts of ATP and lactate
✔✔Cori Cycle - ✔✔uses the lactate made by fermentation in the liver and uses
gluconeogenesis to covert two lactate to glucose. 2 ATP are made with each cycle but it
uses 6. So the net loss is -4 ATP>
✔✔catabolic pathway - ✔✔those that generate energy by breaking down larger
molecules. Both types of pathways are required for maintaining the cell's energy
balance
