A schematic structure of the subunit of hemerythrin (an oxygen-binding protein from invertebrate animals) is shown to the right.
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?