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6. The tertiary structure in haemoglobin occurs when

  • each polypeptide chain is loosely coiled
  • each polypeptide chain is folded into a precse shape
  • each polypeptide chain is tightly coiled
  • each polypeptide chain sucks up an oxygen molecule... like a hoover

7. At respiring tissues, the oxygen concentration is

  • non existent
  • high
  • low
  • medium

8. At the gas exchange surface, oxygen is...

  • eaten
  • attached
  • used
  • released

9. The primary structure in haemoglobin consists of

  • two polypeptide chains
  • eight polypeptide chains
  • four polypeptide chains
  • one polypeptide chain

10. The carbon dioxide concentration at the gas exchange surface is

  • low
  • non existent
  • high
  • medium

11. Haemoglobins with a low affinity for oxygen

  • take up oxygen more easily but release it less rapidly.
  • take up oxygen less rapidly and release it less rapidly.
  • take up oxygen less easily but release it more rapidly.
  • take up oxygen more easily and release it rapidly.

12. The secondary structure in haemoglobin is when each of the polypeptides chains are

  • joined together by nitrogen bonds
  • folded into a precise shape
  • coiled into a helix
  • broken in half

13. The affinity of haemoglobin for oxygen as the gas exchange surface is

  • non existent
  • low
  • high
  • medium

14. The quaternary structure in haemoglobin is when

  • all four polypeptides are linked together to form an almost spherical molecule.
  • all four polypeptides are coiled together.
  • all four polypeptides are linked together to form a perfect circle.
  • all four polypeptides just randomly link up.