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BioChem C785 - WGU - Module 3 - all questions Answered $8.04   Add to cart

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BioChem C785 - WGU - Module 3 - all questions Answered

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BioChem C785 - WGU - Module 3 - all questions Answered-Hb (hemoglobin) binds to CO (carbon monoxide) with a higher affinity than oxygen and stabilizes the R (relaxed) state - True When hemoglobin changes from the T to the R, it has a high affinity for oxygen - True When hemoglobin changes...

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  • April 24, 2022
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BioChem C785 - WGU - Module 3 - all questions Answered
Hb (hemoglobin) binds to CO (carbon monoxide) with a higher affinity than oxygen
and stabilizes the R (relaxed) state
- True

When hemoglobin changes from the T to the R, it has a high affinity for oxygen
- True

When hemoglobin changes from the R to T, it has a low affinity for oxygen
- True

Cooperatively refers to
- structural changes that increases the affinity for oxygen in hemoglobin

When the oxygen concentration is high, the heme shape is planar. When the oxygen
concentration is low, the heme shape is bent shape.
- True

The Bohr effect is a relationship between hemoglobin's oxygen binding behavior in
conjunction with the pH of the surroundings. When the pH is low, hemoglobin has low
affinity for oxygen and releases oxygen
- True

Bohr effect is a relationship between hemoglobin's oxygen binding behavior in
conjunction with the pH of the surroundings. When the pH is high, hemoglobin has
high affinity for oxygen and binds oxygen.
- True

Relative to the lungs, the pH in the peripheral tissues is lower, because the CO2
generated by metabolism is converted to bicarbonate, which releases proton (H+)
- True

The Bohr effect is a relationship between hemoglobin's oxygen binding behavior in
conjunction with the pH of the surroundings. When the H+ ion concentration increases,
the pH of the solution decreases.
- True

Myoglobin stores oxygen, whereas hemoglobin transports oxygen. Myoglobin has a
higher affinity for oxygen compared to hemoglobin
- True

, Hemoglobin is an oxygen transport protein, whereas myoglobin is an oxygen storage
protein. They exhibit different binding curves when plotted on a graph with total partial
pressure of the oxygen (x-axis) plotted against the percentage saturation of hemoglobin
(y-axis). What pattern of binding curves do these proteins exhibit?
- Hemoglobin has a sigmoidal curve whereas the myoglobin has a hyperbolic curve.

Hemoglobin and myoglobin proteins bind to molecular oxygen. However, the protein
part of the hemoglobin does not bind directly to the oxygen. Instead a specific atom
helps bind the oxygen - - Iron

The symptoms of sickle cell anemia are primarily because red blood cells are
misshaped, due to
- a mutation in the beta hemoglobin gene which leads to the insertion of valine into the
hydrophobic patches on deoxygenated hemoglobin

Relative to the peripheral tissues, the pH in lungs is higher, because
- the protons (H+) that were combined with hemoglobin quickly bind to bicarbonate
(HCO3-) to form CO2; the CO2 is then exhaled

Why is carbon monoxide poisonous?
- it binds hemoglobin 200 times better than oxygen

BPG stabilizes the T (tense) states of hemoglobin
- True

Even though the amino acids sequence between subunits of hemoglobin and myoglobin
are not exactly the same, there are other similarities between the two proteins. Which
level of protein structure is not found in both molecules?
- Quarternary

In the deoxygenated state the heme is bent, where as in the oxygenated state, the heme
is planar.
- True

Fetal hemoglobin binds to oxygen tightly at lower oxygen concentrations since its R
state is the preferred structure.
- True

When blood pH is low, the heme is in bent shape. When the blood pH is high, the heme
is in planar shape.
- True

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