haemaglobin

• describe the structure of haemoglobin

  quaternary structure, has 4 polypeptide chains each containing a haem group of iron
• what is affinity 


  ability of haemoglobin to attract or bind to oxygen
• what is saturation of haemoglobin with oxygen

  haemoglobin holding maximum amount of oxygen it can bind
• what is loading/ association of haemoglobin

  binding of oxygen to haemoglobin
• what is unloading/ dissociation of haemoglobin

  oxygen detaches/ unbinds from haemoglobin
• where is oxygen loaded

  in regions of high partial pressure of oxygen such as alveoli
• where is oxygen unloaded

  in regions of low partial pressure such as respiring tissue
• describe cooperative binding 


  haemoglobin changes shape after the first oxygen binds. after this it is easier for further oxygen to bind.
• what is the bohr effect 


  effect of carbon dioxide
• what side does carbon dioxide cause a shift to and why

  the right meaning the affinity for oxygen decreases as carbon dioxide is acidic so slightly changes shape of haemoglobin
• what has happened when Bohr has shifted to the left

  least acidic conditions, so low partial pressure of carbon dioxide, so there is increased affinity so greater association of oxygen e.g. alveoli
• what happened when Bohr curve shifted right

  most acidic conditions as high partial pressure of carbon dioxide, so there is decreased affinity due to the change in shape, more there is more oxygen dissociation. occurs in respiring tissues where carbon dioxide is produced. this is an advantage as aerobic respiration can continue, so ATP is produced so muscle contractions can continue.
• animals have different haemoglobin so they have different affinity for oxygen as they are adapted to their environments