naseeragani
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Hey, how do haemoglobin molecules differ in terms of function and structure?

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jones107
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you can get different types of haemaglobin (HB) with different oxygen affinities, dont know about structure,
but HB with a very high O2 affinity will hold onto the oxygen for loner, so is found in low oxygen areas and foetus' with normal it just dropps off O2 with increasing concentracions of CO2 (see chloride shift)

with sickle cell anemia th haemaglobin is slightly changed so is a long strand of molecules not jusone in blob, but sickle cell afflicted RBC(red bld cells) are resistant t malaria


you may want to check up on that, but i think its all good
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Flying Cookie
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In adult humans, the most common hemoglobin type is a tetramer (which contains 4 subunit proteins) called hemoglobin A, consisting of two α and two β subunits non-covalently bound. In human infants, the hemoglobin molecule is made up of 2 α chains and 2 γ chains. The gamma chains are gradually replaced by β chains as the infant grows. -Wikipedia
As structure is linked to function, it's expected that the haemoglobin's main property - its affinity to oxygen - changes from one structure to another. Different environments determine whether an organism's haemoglobin evolves as high-affinity or low-affinity. The main factor involved is the partial pressure of oxygen in the air or water (the ppO2). The higher the ppO2, the lower the affinity of the haemoglobin.
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