Oxygen channels and fractal wave-particle duality in the evolution of myoglobin and neuroglobin

The evolution of terrestrial and aquatic globins is dominated by changes in two proximate-distal His channels, here monitored quantitatively by hydropathic waves. These waves reveal allometric functional features inaccessible to single amino acid stereochemical contact models, and even very large all-atom Newtonian simulations. The evolutionary differences between these features between myoglobin and neuroglobin are related to the two oxidation channels through hydropathic wave analysis, which identifies subtle interspecies functional differences inaccessible to traditional size and metabolic scaling studies. Level set analysis involves dynamic synchronization of allometric interactions across entire globins. Amino acid sequences alone show functional differences between species, which reflect basic metabolic differences (for instance, between temperate and tropical fresh water fish, or differing escape strategies of mice and rabbits).