Exam 5: Protein Function

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Describe the cycle of actin-myosin association and disassociation that leads to muscle contraction.

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First,ATP binds to myosin and a cleft in the myosin molecule opens,disrupting the actin-myosin interaction so that the bound actin is released.Second,ATP is hydrolyzed,causing a conformational change in the protein to a "high-energy" state that moves the myosin head and changes its orientation in relation to the actin thin filament.Myosin then binds weakly to an F-actin subunit closer to the Z disk than the one just released.Third,as the phosphate product of ATP hydrolysis is released from myosin,another conformational change occurs in which the myosin cleft closes,strengthening the myosin-actin binding.Fourth,this is followed quickly by a "power stroke" during which the conformation of the myosin head returns to the original resting state,its orientation relative to the bound actin changing so as to pull the tail of the myosin toward the Z disk.ADP is then released to complete the cycle.

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?

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Ka = 1/Kd.The larger the Ka (and hence the smaller the Kd),the higher the affinity of the protein for the ligand.

How does BPG binding to hemoglobin decrease its affinity for oxygen?

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BPG binds to a cavity between the β\beta subunits.It binds preferentially to molecules in the low-affinity T state,thereby stabilizing that conformation.

The fundamental cause of sickle-cell disease is a change in the structure of:

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During muscle contraction,hydrolysis of ATP results in a change in the:

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The energy that is released by the hydrolysis of ATP by actin is used for:

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Describe briefly the two principal models for the cooperative binding of ligands to proteins with multiple binding sites.

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Why is carbon monoxide (CO)toxic to aerobic organisms?

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A monoclonal antibody differs from a polyclonal antibody in that monoclonal antibodies:

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(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.

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An allosteric interaction between a ligand and a protein is one in which:

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Describe briefly the structure of myosin.

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What is the relationship between G-actin and F-actin?

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Which of the following parts of the IgG molecule are not involved in binding to an antigen?

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Which of the following generalizations concerning motor proteins is correct?

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Neuroglobin is a member of the globin family found in neurons.It is a monomeric protein that helps protect the brain from hypoxia (low O2).Identify the correct statement(s)about neuroglobin below. a-It binds O2 with a hyperbolic binding curve. b-It binds O2 with a sigmoidal binding curve. c-It binds O2 with higher affinity than hemoglobin. d-It binds O2 with lower affinity than hemoglobin.

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What properties of antibodies make them useful biochemical reagents? Describe one biochemical application of antibodies (with more than just the name of the technique).

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What fraction of ligand binding sites are occupied ( θ\theta )when [ligand] = Kd? Show your work.

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When oxygen binds to a heme-containing protein,the two open coordination bonds of Fe2+ are occupied by:

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Explain why most multicellular 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.

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