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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.