Which of the following statements is FALSE? In its interaction with hemoglobin, oxygen is: Which of the following best describes the tertiary structure of myoglobin? Which of the following amino acids has the most significant role in the molecular mechanisms of hemoglobin's function? Which of the following statements about 2,3-bisphosphoglycerate (BPG) binding is FALSE? Fetal hemoglobin has a higher affinity for oxygen than maternal hemoglobin

1. Which of the following statements is FALSE? In its interaction with hemoglobin, oxygen is:

a prosthetic group.

2. Which of the following best describes the tertiary structure of myoglobin?

It contains heme, which is slotted into a hydrophobic pocket between -helix E and -helix F.

3. Which of the following amino acids has the most significant role in the molecular mechanisms of hemoglobin's function?

histidine

4. Which of the following statements about 2,3-bisphosphoglycerate (BPG) binding is FALSE?

BPG aids oxygen delivery to tissues by increasing the affinity of myoglobin for oxygen.

5. Fetal hemoglobin has a higher affinity for oxygen than maternal hemoglobin. Which of the following statements correctly outlines the mechanism behind this observation?

In fetal hemoglobin, the residue His143 is mutated to Ser143, and so the protein binds BPG with lower affinity.

6. Which of the following statements correctly describes the interaction between an allosteric protein and an allosteric effector?

The effector binds reversibly at a specific site on one subunit of the protein, causing a global change in conformation.

7. Which of the following statements about sickle cell anemia is FALSE?

Sickle cell anemia is a consequence of a conservative mutation in the β-globin gene.

8. Which of the following triggers the transition from T state to R state (low to high affinity) in hemoglobin?

oxygen binding

9. Which of the following statements about the structure of myoglobin is FALSE?

Myoglobin contains all three types of secondary structure.

10. A newly-identified protein has a sigmoidal curve in a graph of fractional saturation versus ligand concentration. What can be deduced about this protein?

The protein undergoes conformational changes in quaternary structure when the ligand binds.