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Quiz

ch 5

skittlesdx 23 questions

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Questions in this quiz (23)

  1. 1The interactions of ligands with proteins:
    1. Aare relatively nonspecific.
    2. Bare relatively rare in biological systems.
    3. Care usually irreversible.
    4. Dare usually transient.
    5. Eusually result in the inactivation of the proteins.
  2. 2A prosthetic group of a protein is a non-protein structure that is:
    1. Aa ligand of the protein.
    2. Ba part of the secondary structure of the protein.
    3. Ca substrate of the protein.
    4. Dpermanently associated with the protein.
    5. Etransiently bound to the protein.
  3. 3When oxygen binds to a heme-containing protein, the two open coordination bonds of Fe2+ are

    occupied by:
    1. Aone O atom and one amino acid atom.
    2. BB) one O2 molecule and one amino acid atom.
    3. Cone O2 molecule and one heme atom.
    4. Dtwo O atoms.
    5. Etwo O2 molecules.
  4. 4In the binding of oxygen to myoglobin, the relationship between the concentration of oxygen and the
    fraction of binding sites occupied can best be described as:
    1. Ahyperbolic.
    2. Blinear with a negative slope.
    3. Clinear with a positive slope.
    4. Drandom.
    5. Esigmoidal.
  5. 5Which of the following statements about protein-ligand binding is correct?
    1. AThe Ka is equal to the concentration of ligand when all of the binding sites are occupied.
    2. BThe Ka is independent of such conditions as salt concentration and pH.
    3. CThe larger the Ka (association constant), the weaker the affinity.
    4. DThe larger the Ka, the faster is the binding.
    5. EThe larger the Ka, the smaller the Kd (dissociation constant).
  6. 6Myoglobin and the subunits of hemoglobin have:
    1. Ano obvious structural relationship.
    2. Bvery different primary and tertiary structures.
    3. Cvery similar primary and tertiary structures.
    4. Dvery similar primary structures, but different tertiary structures.
    5. Every similar tertiary structures, but different primary structures.
  7. 7An allosteric interaction between a ligand and a protein is one in which:
    1. Abinding of a molecule to a binding site affects binding of additional molecules to the same site.
    2. Bbinding of a molecule to a binding site affects binding properties of another site on the protein.
    3. Cbinding of the ligand to the protein is covalent.
    4. Dmultiple molecules of the same ligand can bind to the same binding site.
    5. Etwo different ligands can bind to the same binding site.
  8. 8In hemoglobin, the transition from T state to R state (low to high affinity) is triggered by:
    1. AFe2+ binding.
    2. Bheme binding.
    3. Coxygen binding.
    4. Dsubunit association.
    5. Esubunit dissociation.
  9. 9Which of the following is not correct concerning 2,3-bisphosphoglycerate (BPG)?
    1. AIt binds at a distance from the heme groups of hemoglobin.
    2. BIt binds with lower affinity to fetal hemoglobin than to adult hemoglobin.
    3. CIt increases the affinity of hemoglobin for oxygen.
    4. DIt is an allosteric modulator.
    5. EIt is normally found associated with the hemoglobin extracted from red blood cells.
  10. 10Which of the following is not correct concerning cooperative binding of a ligand to a protein?
    1. AIt is usually a form of allosteric interaction.
    2. BIt is usually associated with proteins with multiple subunits.
    3. CIt rarely occurs in enzymes.
    4. DIt results in a nonlinear Hill Plot.
    5. EIt results in a sigmoidal binding curve.

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Quiz on ch 5, created by skittlesdx on 08/07/2015.
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