Cooperativity
About the Lecture
The lecture Cooperativity by Kevin Ahern, PhD is from the course Amino Acid Metabolism.
Included Quiz Questions
Which of the following is true regarding the cooperativity in hemoglobin?
- The binding of the first oxygen is the least favorable oxygen binding.
- The binding of the last oxygen is the least favorable oxygen binding.
- The binding of oxygen turns hemoglobin into the T-state.
- In the R-state, hemoglobin can carry three oxygen molecules.
- Once the first globin changes to the R-state, all other globins change to the R-state.
In what way does the myoglobin bind to oxygen?
- With higher affinity than hemoglobin
- To the same extent as hemoglobin
- With lower affinity than hemoglobin
- Irreversibly
- Through a process call cooperativity
Which of the following is NOT true regarding the phenomenon of cooperativity?
- Myoglobin changes from a relaxed to a tight state at high oxygen concentration levels, favoring oxygen binding.
- Cooperativity is displayed by systems having dependently acting identical or near-identical subunits.
- Cooperativity of hemoglobin toward oxygen binding in the lungs shows conformational changes from the T state to the R state.
- The binding of oxygen on the hemoglobin molecule enhances the affinity of adjacent binding sites for oxygen.
- The binding of a ligand to one of the binding sites increases or decreases the affinity of the other binding sites to the ligand.
Which of the following are NOT correctly matched?
- Cooperativity — binding of oxygen to myoglobin
- Oxygen affinity curve for hemoglobin — Sigmoidal
- Binding of oxygen to myoglobin — Low concentrations of oxygen
- Oxygen affinity curve for myoglobin — Hyperbolic
- Oxygen and hemoglobin — Cooperativity
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Author of lecture Cooperativity
Kevin Ahern, PhD
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