This engaging lesson looks at the role of haemoglobin in transporting oxygen and carbon dioxide and compares the dissociation curves for foetal and adult haemoglobin. The detailed PowerPoint has been designed to cover points 3.1.2 (i & j) of the OCR A-level Biology A specification and includes references to the role of carbonic anhydrase and the formation of haemoglobinic acid and carbaminohaemoglobin.
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. At this point, foetal haemoglobin and its differing affinity of oxygen is introduced and students are challenged to predict whether this affinity will be higher or lower than adult haemoglobin and to represent this on their dissociation curve.
The remainder of the lesson looks at the different ways that carbon dioxide is transported around the body that involve haemoglobin. Time is taken to look at the dissociation of carbonic acid into hydrogen ions so that students can understand how this will affect the affinity of haemoglobin for oxygen in an upcoming lesson on the Bohr effect.
It is estimated that it will take in excess of 2 hours of A-level teaching time to cover the detail of these two specification points as covered in this lesson
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