A set of thorough and concise notes created and used by an A* grade student to revise Mass transport (ch 7 from the A Level AQA Biology course). The notes are detailed and clearly explain the topic by breaking each process down into steps. It includes clear and detailed diagrams and includes all co...
,Structure of haemoglobin molecule
• Haemoglobins are similar across a range of organisms: all have this
same basic structure…
• Has a quaternary structure, built up from primary [amino acids]
secondary [helixes] tertiary [precise 3d shape = necessary to
load/unload O2] quaternary [4 polypeptides linked, each associate
to a haem group Fe2+]
,Loading and unloading O2
• Loading, or associating, is when haemoglobin binds with O2 in the
lungs/alveolar capillaries
• Unloading, or dissociating, is when haemoglobin releases O2 into th
tissues in capillaries
• Haemoglobins with high affinity for O2 = load O2 more easily but
struggle to unload it, whereas low affinity = harder to load O2 but
easier to unload
, The role of haemoglobin
• Transport O2
• Need to be efficient by readily associating in lungs during gas
exchange, and readily dissociating in the tissues
• To do this, haemoglobin changes its affinity for oxygen based on th
conditions e.g. level of CO2 as they change the shape of the molecu
changes
High CO2 – CO2 dissolves in plasma – lowers pH – conformational
change in haemoglobin -
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