BioChem C785 - WGU - Module 3 - all
questions
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? –
questions
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? –
