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______of the world's human population carries an inherited variant hemoglobin gene

Biology

  1. ______of the world's human population carries an inherited variant hemoglobin gene.
    A
    Option A: 75%
    B
    Option B: 90%
    C
    Option C: 25%
    D
    Option D: 5%
    E
    Option E: 50%
  2. Hemoglobin S, the variant responsible for the misshapen red blood cells characteristic of the disease sickle-cell anemia, is potentially advantageous to heterozygotes because it confers some level of resistance to the disease _________.
    A
    Option A: rickets
    B
    Option B: polycythemia
    C
    Option C: cyanosis
    D
    Option D: malaria
    E
    Option E: AIDS
  3. In sickle-cell anemia, the negatively charged glutamic acid residue is replaced by the neutral amino acid ____________.
    A
    Option A: adenosine
    B
    Option B: lysine
    C
    Option C: glycine
    D
    Option D: valine
    E
    Option E: tyrosine
  4. Some abnormal hemoglobins have Hill coefficients that are ______ that of normal hemoglobin, indicating that their ability to bind oxygen cooperatively has been compromised.
    A
    Option A: much greater than
    B
    Option B: less than
    C
    Option C: about equal to
    D
    Option D: greater than
    E
    Option E: The correct answer cannot be determined from the information given.
  5. During the T to R conformational shift, Fe(II) drags the F helix via a bond to the side chain of ________.
    A
    Option A: Leu F4
    B
    Option B: Leu F7
    C
    Option C: Leu FG3
    D
    Option D: His F8
    E
    Option E: Val FG5
  6. The reaction of carbonic anhydrase catalyzes
    A
    Option A: the reduction of carbon dioxide with the concomitant consumption of protons.
    B
    Option B: the hydrolysis of carbamates with the concomitant consumption of protons.
    C
    Option C: the hydration of bicarbonate, resulting in the formation of carbonic acid.
    D
    Option D: the hydration of carbon dioxide, forming bicarbonate and protons.
    E
    Option E: the formation of carbamates with the concomitant release of protons.
  7. Why is the decreased affinity of fetal hemoglobin for BPG advantageous?
    A
    Option A: Decreased BPG binding biases the fetal hemoglobin toward the R state.
    B
    Option B: BPG is available to bind to fetal myoglobin, helping to release O2 in fetal muscle tissue.
    C
    Option C: None of the above.
    D
    Option D: More free BPG is available to bind to adult hemoglobin, resulting in a shift to the R state.
    E
    Option E: With fewer BPG molecules bound there are more heme residues available for O2 binding.
  8. BPG stands for
    A
    Option A: boronylphenylglutamate.
    B
    Option B: biphenylglycine.
    C
    Option C: bisphosphoglycerate.
    D
    Option D: betapropylglutamine.
    E
    Option E: bisphenylglycerol.
  9. Which of the following statements about the symmetry model of allosterism is not true?
    A
    Option A: the oligomer can exist in two conformational states, which are in equilibrium.
    B
    Option B: the ligand can bind to a subunit in either conformation.
    C
    Option C: the molecular symmetry of the protein is conserved during the conformational change.
    D
    Option D: the protein is an oligomer of symmetrically (or pseudosymmetrically) related subunits.
    E
    Option E: none of the above.
  10. The rearrangement of T state hemoglobin to the R state
    A
    Option A: increases the ion pairing interactions of the C-terminal amino acids.
    B
    Option B: opens a central cavity for BPG binding.
    C
    Option C: occurs in each protein subunit independently when its heme binds oxygen.
    D
    Option D: involves the movement of the Fe(II) into the heme plane.
    E
    Option E: requires the binding of at least three oxygen molecules.

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