Myoglobin hydrophobic association

Hemoglobin Hydrophobic Association of Four Myoglobin-Like Proteins... 

Figure 7.9. Mean residue hydropho-bicity plots of the a-chain (A) and the P-chain (B) of hemoglobin and of myoglobin (C). The strong hydrophobidty peaks just above 100 residues are responsible for stable formation of the a P dimer. The strong hydrophobidty peaks near 40 residues may be considered part of the switch region. TTiese hydrophobic residues provide an arc for hydrophobic association at the a P -a P interface. By the consilient mechanism, decreased heme hydropho-bicity on oxygen binding relaxes this inter-dimer hydrophobic assodation and allows the T R transition, as shown in Figure 7.10, to occur. This is further visualized in Figure 7.18 as discussed in the text. See text for further discussion.

---