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Questions and Answers
Which part of myoglobin binds oxygen reversibly?
Which part of myoglobin binds oxygen reversibly?
- Globin portion
- Fe3+ ion
- Porphyrin ring (correct)
- Nitrogen atoms
What is the role of the His (histidine) residues in myoglobin's structure?
What is the role of the His (histidine) residues in myoglobin's structure?
- Bind CO molecules
- Increase oxygen solubility
- Facilitate protein folding
- Help prevent conversion of heme iron to Fe3+ state (correct)
Which part of myoglobin contains both polar and non-polar amino acids?
Which part of myoglobin contains both polar and non-polar amino acids?
- His E7 and His F8
- Alpha-helix
- Heme group
- Exterior residues (correct)
What is the main function of the globin portion in myoglobin?
What is the main function of the globin portion in myoglobin?
Why does heme iron in myoglobin bind oxygen reversibly?
Why does heme iron in myoglobin bind oxygen reversibly?
Which compound binds to heme with higher affinity than oxygen, leading to toxicity?
Which compound binds to heme with higher affinity than oxygen, leading to toxicity?
What is the role of His 64 in myoglobin in relation to carbon monoxide binding?
What is the role of His 64 in myoglobin in relation to carbon monoxide binding?
What is the formula for calculating the affinity of a ligand to a protein in terms of dissociation constant (Kd)?
What is the formula for calculating the affinity of a ligand to a protein in terms of dissociation constant (Kd)?
What does the Oxygen Binding Curve for Myoglobin indicate?
What does the Oxygen Binding Curve for Myoglobin indicate?
Which factor contributes to the high affinity of hemoglobin for oxygen?
Which factor contributes to the high affinity of hemoglobin for oxygen?
What structural changes occur in hemoglobin upon oxygen binding?
What structural changes occur in hemoglobin upon oxygen binding?
What distinguishes hemoglobin from myoglobin primarily due to quaternary structure differences?
What distinguishes hemoglobin from myoglobin primarily due to quaternary structure differences?
What effect does the rotation and sliding of the ab subunit have on the pocket between the b subunits?
What effect does the rotation and sliding of the ab subunit have on the pocket between the b subunits?
In what state does hemoglobin have a higher affinity for O2?
In what state does hemoglobin have a higher affinity for O2?
What is an example of an allosteric effect in hemoglobin?
What is an example of an allosteric effect in hemoglobin?
What is the primary characteristic of cooperative binding of oxygen in hemoglobin?
What is the primary characteristic of cooperative binding of oxygen in hemoglobin?
Which molecule binds weakly to deoxyhemoglobin as part of the T R transition?
Which molecule binds weakly to deoxyhemoglobin as part of the T R transition?
What equation is used to describe the binding of oxygen to myoglobin and hemoglobin in Hill plots?
What equation is used to describe the binding of oxygen to myoglobin and hemoglobin in Hill plots?
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