Protein Function: Transport, Storage, and Enzymes
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Questions and Answers

Which part of myoglobin binds oxygen reversibly?

  • Globin portion
  • Fe3+ ion
  • Porphyrin ring (correct)
  • Nitrogen atoms
  • What is the role of the His (histidine) residues in myoglobin's structure?

  • Bind CO molecules
  • Increase oxygen solubility
  • Facilitate protein folding
  • Help prevent conversion of heme iron to Fe3+ state (correct)
  • Which part of myoglobin contains both polar and non-polar amino acids?

  • His E7 and His F8
  • Alpha-helix
  • Heme group
  • Exterior residues (correct)
  • What is the main function of the globin portion in myoglobin?

    <p>Facilitate O2 binding to Fe2+ ion</p> Signup and view all the answers

    Why does heme iron in myoglobin bind oxygen reversibly?

    <p>Due to nitrogen atoms in the porphyrin ring</p> Signup and view all the answers

    Which compound binds to heme with higher affinity than oxygen, leading to toxicity?

    <p>$CO (carbon monoxide)$</p> Signup and view all the answers

    What is the role of His 64 in myoglobin in relation to carbon monoxide binding?

    <p>His 64 prevents the linear binding of carbon monoxide to heme iron.</p> Signup and view all the answers

    What is the formula for calculating the affinity of a ligand to a protein in terms of dissociation constant (Kd)?

    <p>Kd = [P] [L]/[PL]</p> Signup and view all the answers

    What does the Oxygen Binding Curve for Myoglobin indicate?

    <p>The relationship between oxygen concentration and myoglobin saturation is hyperbolic.</p> Signup and view all the answers

    Which factor contributes to the high affinity of hemoglobin for oxygen?

    <p>Low P50 value</p> Signup and view all the answers

    What structural changes occur in hemoglobin upon oxygen binding?

    <p>Transition from R state to T state resulting in conformational stability.</p> Signup and view all the answers

    What distinguishes hemoglobin from myoglobin primarily due to quaternary structure differences?

    <p>Cooperative binding to small molecules like CO2 and H+</p> Signup and view all the answers

    What effect does the rotation and sliding of the ab subunit have on the pocket between the b subunits?

    <p>Narrows the pocket</p> Signup and view all the answers

    In what state does hemoglobin have a higher affinity for O2?

    <p>Oxy-hemoglobin</p> Signup and view all the answers

    What is an example of an allosteric effect in hemoglobin?

    <p>T R transition</p> Signup and view all the answers

    What is the primary characteristic of cooperative binding of oxygen in hemoglobin?

    <p>Sigmoid (cooperative) binding curve</p> Signup and view all the answers

    Which molecule binds weakly to deoxyhemoglobin as part of the T R transition?

    <p>First O2 molecule</p> Signup and view all the answers

    What equation is used to describe the binding of oxygen to myoglobin and hemoglobin in Hill plots?

    <p>[PLn]/[P][L]n = Ka</p> Signup and view all the answers

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