unit 3; haemoglobin and mass transport Flashcards

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1
Q

primary structure of haemoglobin

A

sequences of amino acids in the 4 polypeptide chains

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2
Q

secondary structure of haemoglobin

A

each polypeptide chain coiled into alpha helix using hydrogen bonds

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3
Q

tertiary structure of haemoglobin

A

active site of protein is formed by folding of polypeptide chains

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4
Q

quaternary structure of haemoglobin

A

4 chains linked, each associated with a haem group

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5
Q

what is positive cooperativity

A

easier for oxygen to bind after previous oxygen binds- except for last

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6
Q

explain the affinity when the oxygen disassociation curve is further to the left

A

greater affinity for oxygen, oxygen will unload less easily

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7
Q

explain the affinity when the oxygen disassociation curve is further to the right

A

lower affinity for oxygen, oxygen will unload more easily

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8
Q

explain the Bohr effect

A

the greater conc of carbon dixoide the lower the affinity for oxygen- carbonic acid changes active site

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