This engaging lesson looks at the structure of the quaternary protein, haemoglobin, and describes its role with red blood cells in the transport of oxygen. The PowerPoint has been designed to cover the first part of point 3.4.1 of the AQA A-level Biology specification and explains how the cooperative nature of binding results in a loading of each molecule with 4 oxygen molecules and describes how it is unloaded at the respiring cells too.
The lesson begins with a version of the quiz show Pointless to introduce haemotology as the study of the blood conditions. Students are told that haemoglobin has a quaternary structure and are challenged to use their prior knowledge of biological molecules to determine what this means for the protein. They will learn that each of the 4 polypeptide chains contains a haem group with an iron ion attached and that it is this group which has a high affinity for oxygen. Time is taken to discuss how this protein must be able to load (and unload) oxygen as well as transport the molecules to the respiring tissues. Students will plot the oxyhaemoglobin dissociation curve and the S-shaped curve is used to encourage discussions about the ease with which haemoglobin loads each molecule. Students will learn that a conformational change upon binding of the first oxygen leads to it being easier to bind future oxygens and that this is known as cooperative binding.
This lesson has been written to tie in with the other uploaded lesson on the Bohr effect.
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Topic 3: Organisms exchange substances with their environment (AQA A-level Biology)
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