Oxygen Channels and Fractal Wave-Particle Duality in the Evolution of Myoglobin and Neuroglobin

TL;DR

This study uses hydropathic wave analysis to uncover subtle evolutionary differences in globin proteins related to oxygen channels, revealing functional features beyond traditional models and simulations.

Contribution

It introduces hydropathic wave analysis as a novel approach to study globin evolution and functional differences in oxygen channels.

Findings

Hydropathic waves reveal allometric functional features in globins.

Differences between myoglobin and neuroglobin relate to oxidation channels.

Analysis uncovers interspecies functional differences inaccessible to traditional methods.

Abstract

The evolution of terrestrial and aquatic wild type (WT) globins is dominated by changes in two proximate - distal Histidine ligand exit 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. Our analysis involves dynamic synchronization of allometric interactions across entire globins.