Haemoglobin

Bee Brittain
Flashcards by Bee Brittain, updated more than 1 year ago
Bee Brittain
Created by Bee Brittain about 5 years ago
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AS - Level Biology (7 - Mass Transport) Flashcards on Haemoglobin, created by Bee Brittain on 03/16/2016.

Resource summary

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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