2268531
Description
Flashcards by Charlotte Hewson, updated more than 1 year ago
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Created by Charlotte Hewson
about 9 years ago
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| Question | Answer |
| what is the primary structure of haemoglobin? | four polypeptide chains |
| what is the secondary structure of haemoglobin? | each polypeptide chain is wound into a helix |
| what is the tertiary structure of haemoglobin? | each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen |
| what is the quaternary structure of haemoglobin? | -all four polypeptides are linked together to form an almost spherical molecule. -each polypeptide is associated with a haem group. |
| what ion is contained within the haem group? | ferrous ion (Fe2+) |
| how many molecules can be combined to one haemoglobin molecule? | 4 |
| how many oxygen atoms can be combined on one haemoglobin? | 8 (because each oxygen molecule has 2 oxygen atoms) |
| what is haemoglobins main role? | to transport oxygen |
| how is haemoglobin efficient at transporting oxygen? | -readily associate with oxygen at the surface where gas exchange takes place -readily dissociate from oxygen at the tissues that need it. |
| why are there different types of haemoglobin? | high affinity - take oxygen easily and release less readily low affinity - take up less easily and release readily |
| what type of haemoglobin would an organism living in an environment with little oxygen need? | high affinity |
| what type of haemoglobin would an organism with high metabolic rate need? | low affinity provided there is sufficient oxygen in the air. |
| what is the process called where haemoglobin combines with oxygen? | loading or associating |
| where does loading/associating happen in humans? | the lungs |
| what is the name of the process in which haemoglobin releases the oxygen? | unloading or dissociating |
| where does dissociation/unloading occur in humans? | in the tissues |
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