A schematic structure of the subunit ot hemerythrin (an oxygen-binding protein from invertebrate animals) is shown below.
(a) It has been found that in some of the α-helical regions of hemerythrin, about every third or fourth amino acid residue is a hydrophobic one. Suggest a structural reason for this finding.
(b) What would be the effect of a mutation that placed a proline residue at point A in the structure?
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