20 Questions
What is the physiologically important role of selective enhancement of affinity in globins?
It helps prevent poisoning by CO generated from metabolism and our industrial-age environment.
How does the binding of oxygen to the heme in myoglobin depend on the protein structure?
It depends on molecular motions or 'breathing' in the protein structure.
Why is it important for the protein structure to have transient cavities?
Transient cavities allow oxygen to move in and out of the heme pocket.
What role does the distal His residue play in myoglobin?
The distal His acts as a gate to control access to one major pocket near the heme iron.
How does the pocket near the heme iron in myoglobin open and close?
The pocket opens and closes through the rotation of the distal His residue on a nanosecond time scale.
What is the main function of hemoglobin in animals?
Hemoglobin transports oxygen in blood.
What is the size and shape of normal human erythrocytes?
Normal human erythrocytes are small, biconcave disks.
What are precursor stem cells for erythrocytes called?
Precursor stem cells for erythrocytes are called hemocytoblasts.
What happens to the organelles of daughter cells during the maturation process of erythrocytes?
Daughter cells produce large amounts of hemoglobin and then lose their organelles.
How is most of the oxygen carried by whole blood in animals transported?
Most of the oxygen carried by whole blood in animals is bound and transported by hemoglobin in erythrocytes.
Which of the following is true about the selective enhancement of affinity in globins?
It helps prevent poisoning by the CO that is generated in large amounts by our industrial-age environment.
What is the role of the distal His residue in myoglobin?
It controls access to one major pocket near the heme iron.
What is the main function of hemoglobin in animals?
Transporting oxygen in the blood.
Why is it important for the protein structure to have transient cavities?
To allow oxygen to move from the surrounding solution to the ligand-binding site.
How does the pocket near the heme iron in myoglobin open and close?
By the rotation of the distal His residue.
What happens to the organelles of daughter cells during the maturation process of erythrocytes?
They are lost.
What is the size and shape of normal human erythrocytes?
Small and biconcave disks.
How is most of the oxygen carried by whole blood in animals transported?
By hemoglobin in erythrocytes.
What is the physiological importance of the selective enhancement of affinity in globins?
It helps prevent poisoning by the CO that is generated in small amounts from metabolism and that is sometimes generated in larger amounts by our industrial-age environment.
How does the binding of oxygen to the heme in myoglobin depend on the protein structure?
It depends on molecular motions, or 'breathing,' in the protein structure.
Quiz: Protein-Ligand Binding and Dissociation Constants Test your knowledge on protein-ligand binding and dissociation constants with this quiz. Learn about the concept of Y representing the fraction of binding sites occupied by a ligand and how the concentration of ligand at which half the binding sites are occupied is the dissociation constant. Explore examples and understand the relationship between ligand concentration and affinity for different proteins.
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