Haemoglobin is a tetramer made up of two α-globin and two β-globin
chains. Each chain contains many α-helices,
several loops and a haem group, with an iron group in the middle that binds
oxygen (fig. 2). The whole structure of the protein is key to its
function, however some helices are of particular importance to this
study. Helices G, H and the FG loop from the α-globin and helices C, G and the
FG loop from the β-globin all contain residues that are required for binding of
haptoglobin to form the complex.
There is no picture for figure 2. Its hard to imagine the structure of the protein. Need more information to describe haemoglobin like how it binds to oxygen.
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