unit 3; haemoglobin and mass transport Flashcards
primary structure of haemoglobin
sequences of amino acids in the 4 polypeptide chains
secondary structure of haemoglobin
each polypeptide chain coiled into alpha helix using hydrogen bonds
tertiary structure of haemoglobin
active site of protein is formed by folding of polypeptide chains
quaternary structure of haemoglobin
4 chains linked, each associated with a haem group
what is positive cooperativity
easier for oxygen to bind after previous oxygen binds- except for last
explain the affinity when the oxygen disassociation curve is further to the left
greater affinity for oxygen, oxygen will unload less easily
explain the affinity when the oxygen disassociation curve is further to the right
lower affinity for oxygen, oxygen will unload more easily
explain the Bohr effect
the greater conc of carbon dixoide the lower the affinity for oxygen- carbonic acid changes active site