by Kevin Ahern, PhD

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    About the Lecture

    The lecture Cooperativity by Kevin Ahern, PhD is from the course Amino Acid Metabolism.

    Included Quiz Questions

    1. The binding of the first oxygen is the least favorable oxygen binding
    2. The binding of the last oxygen is the least favorable oxygen binding
    3. The binding of oxygen turns hemoglobin into the T-state
    4. None of the answers are true
    5. All of the answers are true
    1. Non-cooperatively
    2. To the same extent as hemoglobin at high oxygen concentration and at very low
    3. With high affinity at low and high concentrations
    4. Oxygen concentration
    5. None of the answers are true
    1. Myoglobin changes from a relaxed to a tight state at high concentration levels of oxygen and hence favors the binding of oxygen to it.
    2. Cooperativity phenomenon is displayed by the systems having dependently acting identical or near-identical subunits
    3. The cooperativity in the hemoglobin towards oxygen binding in the lungs shows conformational changes from T state to R state
    4. The binding of oxygen with one binding site on the hemoglobin molecule enhances the affinity of other three binding sites for the oxygen
    5. The binding of a ligand to one of the binding site increases or decreases the affinity of the other binding sites to the ligand molecules
    1. Concerted model of cooperativity — Myoglobin and oxygen binding
    2. Oxygen affinity curve for hemoglobin — Sigmoidal
    3. Glyceraldehyde-3-phosphate and glyceraldehyde-3-phosphate dehydrogenase — Negative cooperativity
    4. Oxygen affinity curve for myoglobin — Hyperbolic
    5. Oxygen and hemoglobin — Positive cooperativity

    Author of lecture Cooperativity

     Kevin Ahern, PhD

    Kevin Ahern, PhD

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