BIOCHEM C785 - WGU – EVERYTHING ABOUT MODULE 3 PRACTICE
SOLUTION
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
SOLUTION
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
