Chapter 7 - Mass transport Flashcards
(163 cards)
where is haemoglobin found
inside red blood cells
what is haemoglobin made of
protein
what type of structure does haemoglobin have
quaternary
what is the primary structure of haemoglobin
the sequence of amino acids in the four polypeptide chains
what is the secondary structure of haemoglobin
each of the polypeptide chains are made into a helix
how many polypeptide chains are there in haemoglobin
4
what is the tertiary structure of haemoglobin
each polypeptide chain is folded into a precise shape
what is the quaternary structure of haemoglobin
the four polypeptide chains are like together. each polypeptide chain is associated with a ham group (a Fe2+ ion) and so the molecule can carry 4 oxygen molecules
what does a ham group contain
a ferrous fe2+ ion
what is the name of the process of binding with oxygen
loading or associating
what is the name of the process of haemoglobin releasing oxygen
unloading or dissociating
where does association with oxygen take place
lungs
where does dissociation of oxygen take place
tissues
what does affinity mean
tendency to combine with
does haemoglobin have a high or low affinity for oxygen
high- it combines with it easily but releases it less easily
what does haemoglobin form when it associated with oxygen
oxyhemoglobin
what properties does haemoglobin have that makes it successful at transporting oxygen
it readily binds to oxygen in the lungs and readily dissociates with oxygen in the tissues
how does haemoglobin obtain its contradicting properties
its tertiary structure so therefore the shape of the active site change under certain conditions like carbon dioxide concentrations
what is partial pressure
a measure of oxygen concentration
when will oxyhemoglobin release its oxygen
when there is a low concentration of oxygen
why do different haemoglobin have different affinities for oxygen
the DNA base sequence differs between species. as a result of the mRNA and tRNA sequences will be different too. Therefore, the amino acid sequence constructers by the ribosomes will be different. Bonds will form in different places and so the tertiary and quaternary structures will beg different. This impacts the haemoglobins ability to bind to oxygen
what is an oxygen dissociation curve
it shows how saturate haemoglobin is with oxygen at any given partial pressure
why is the gradient of the oxygen dissociation curve shallow initially
at low oxygen concentrations the haemoglobin has a low low affinity for oxygen so it releases it other than associating with it. this is because it Changes its shape to make it harder for oxygen to bind to it.
What happens once the first molecule of oxygen has bonded to the haemoglobin?
The binding of the oxygen molecule makes the haemoglobin change its shape so that is easier for the other haem groups to bind to an oxygen molecule