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    Answer Questions5 1

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    yo-cheng
    The document contains short answer questions about reversible binding of proteins to ligands, specifically oxygen-binding proteins. It includes questions about induced fit, the roles of heme and proteins in oxygen binding, determining association constants, the relationship between association and dissociation constants, factors that influence the relative affinity of heme for oxygen and carbon monoxide, the structural differences between myoglobin and hemoglobin in relation to their functions, cooperative ligand binding, models of cooperative binding, how BPG binding decreases hemoglobin's affinity for oxygen, and the Bohr effect.

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    Answer Questions5 1

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    yo-cheng
    2K views3 pages
    The document contains short answer questions about reversible binding of proteins to ligands, specifically oxygen-binding proteins. It includes questions about induced fit, the roles of heme and proteins in oxygen binding, determining association constants, the relationship between association and dissociation constants, factors that influence the relative affinity of heme for oxygen and carbon monoxide, the structural differences between myoglobin and hemoglobin in relation to their functions, cooperative ligand binding, models of cooperative binding, how BPG binding decreases hemoglobin's affinity for oxygen, and the Bohr effect.

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    The document contains short answer questions about reversible binding of proteins to ligands, specifically oxygen-binding proteins. It includes questions about induced fit, the roles of heme and proteins in oxygen binding, determining association constants, the relationship between association and dissociation constants, factors that influence the relative affinity of heme for oxygen and carbon monoxide, the structural differences between myoglobin and hemoglobin in relation to their functions, cooperative ligand binding, models of cooperative binding, how BPG binding decreases hemoglobin's affinity for oxygen, and the Bohr effect.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    2K views3 pages

    Answer Questions5 1

    Uploaded by

    yo-cheng
    The document contains short answer questions about reversible binding of proteins to ligands, specifically oxygen-binding proteins. It includes questions about induced fit, the roles of heme and proteins in oxygen binding, determining association constants, the relationship between association and dissociation constants, factors that influence the relative affinity of heme for oxygen and carbon monoxide, the structural differences between myoglobin and hemoglobin in relation to their functions, cooperative ligand binding, models of cooperative binding, how BPG binding decreases hemoglobin's affinity for oxygen, and the Bohr effect.

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    Short Answer Questions Made by yo-cheng

    Chapter 5.1 僅供參考 不負責任


    1. Reversible binding of a protein to a ligand: oxygen-binding proteins
    Page: 158
    Describe the concept of “induced fit” in ligand-protein binding.
    The binding of a protein and ligand is often coupled to a conformational change in
    protein that makes the binding site more complementary to lighad , permitting tighter
    bindin.

    2. Reversible binding of a protein to a ligand: oxygen-binding proteins


    Page: 158
    Explain why most multi-cellular organisms use an iron-containing protein for
    oxygen binding rather than free Fe2+. Your answer should include an
    explanation of (a) the role of heme and (b) the role of the protein itself.
    (a)Free ion promotes the formation of highly reactive oxygen species that can
    damage DNA and other macro molecules, so ion is incorporated into a protein
    bound-prosthetic group called heme to make it less reactive ;
    (b)Oxygen is poorly soluble in aqueous solution, so larger, multi-cellular animals
    depend on the evolution of protein that could transport and storage oxygen.

    3. Reversible binding of a protein to a ligand: oxygen-binding proteins


    Pages: 160.161
    Describe how you would determine the Ka (association constant) for a ligand and
    a protein.

    4. Reversible binding of a protein to a ligand: oxygen-binding proteins


    Page: 160
    For the binding of a ligand to a protein, what is the relationship between the Ka
    (association constant), the Kd (dissociation constant), and the affinity of the
    protein for the ligand?
    5. Reversible binding of a protein to a ligand: oxygen-binding proteins
    Page: 162
    Explain briefly why the relative affinity of heme for oxygen and carbon
    monoxide is changed by the presence of the myoglobin protein.
    Carbon monoxide binds to free heme with the CO axis perpendicular to the plane of
    the porphyrin ring. When binding to the heme in myoglobin, CO is forced to adopt a
    slight angle because the perpendicular arrangement is sterically blocked by His E7,
    the distal His. This effect weakens the binding of CO to myoglobin.

    6. Reversible binding of a protein to a ligand: oxygen-binding proteins


    Pages: 161, 166
    Explain why the structure of myoglobin makes it function well as an
    oxygen-storage protein whereas the structure of hemoglobin makes it function
    well as an oxygen-transport protein.
    Myoglobin with its hyperbolic binding curve for oxygen, is relatively insensitive to
    small changes in the concentration of dissolved oxygen and so functions well as an
    oxygen-storage protein. (eight α-helix segments )
    Hemoglobin, with its multiple subunits and O2-binding sites, is better suited to
    oxygen transport. (four α and β segments)

    7. Reversible binding of a protein to a ligand: oxygen-binding proteins


    (a) What are the characteristics of an allosteric protein?
    (b) How can cooperative ligand binding be described quantitatively?
    (a)An allosteric protein is one in which the binding of a ligand to one site affects
    the binding properties of another site on the same protein.
    (b)

    8. Reversible binding of a protein to a ligand: oxygen-binding proteins


    Pages: 167.170
    Describe briefly the two principal models for the cooperative binding of ligands
    to proteins with multiple binding sites
    1. MWC(concerted): all the subunit are the same.
    2. Sequential model: individual subunit conformation, can gradually change.
    9. Reversible binding of a protein to a ligand: oxygen-binding proteins
    Pages: 171.172
    How does BPG binding to hemoglobin decrease its affinity for oxygen?
    BPG lowers hemoglobin’s affinity for oxygen by stabilizing the T state.

    10. Reversible binding of a protein to a ligand: oxygen-binding proteins


    Page: 170
    (a) What is the effect of pH on the binding of oxygen to hemoglobin (the Bohr
    Effect)?
    (b) Briefly describe the mechanism of this effect.

    At the relatively low pH and high CO2 concentration of peripheral tissues, the
    affinity of hemoglobin for oxygen decreases as H+ and CO2 are bound, and O2 is
    released to the tissues. Conversely, in the capillaries of the lung, as CO2 is excreted
    and the blood pH consequently rises, the affinity of hemoglobin for oxygen increases
    and the protein binds more O2 for transport to the peripheral tissues. This effect of pH
    and CO2concentration on the binding and release of oxygen by hemoglobin is called
    the Bohr effect.

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