4874606
Description
Flashcards by Bee Brittain, updated more than 1 year ago
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Created by Bee Brittain
about 8 years ago
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| Question | Answer |
| Haemoglobin is a protein molecule. This means it has four stages of protein structure. Name them. | Primary Secondary Tertiary Quarternany |
| Describe the Primary Structure of a Haemoglobin. | It is the sequence of amino acids in each polypeptide chain |
| Describe the Secondary Structure of haemoglobin. | The secondary structure, is where each polypeptide chain, coils into a helix due to hydrogen bonds forming between the animo acids |
| Describe the Tertiary Structure of Haemoglobin. | The tertiary structure is where each polypeptide chain is folded into a precise shape - this is an important factor in its ability to carry oxygen/its oxygen affinity |
| Describe the quaternary structure of haemoglobin. | Each polypeptide chain is linked together, forming an almost spherical shape. Each chain is associated with a haem group, which has its own Ferrous (Fe2+) ion. Each ion can carry one molecule of oxygen. |
| How many molecules of Oxygen can one haemoglobin carry? | 4 molecules of oxygen |
| Where does haemoglobin associate/load oxygen? | In the lungs at the surface where gaseous exchange takes place |
| Where does haemoglobin dissociate/unload oxygen? | At the respiring tissues that need it |
| The association of oxygen changes if its shape does. In the presence of CO2 what happens to haemoglobin? How does this help? | In the presence of CO2, haemoglobin binds more loosely to oxygen, this means it dissociates more readily and easily, releasing oxygen |
| Why are there different types of haemoglobin in different organisms? | Each species has a slightly different haemoglobin as there are variation in the sequence of amino acid in the haemoglobin's primary structure, meaning that all the further structures will also change |
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