Hemoglobin Strain Field Waves and Allometric Functionality

Abstract

Hemoglobin (Hgb) forms tetramers (dimerized dimers), which enhance its globular stability and may also facilitate small gas molecule transport, as shown by recent all-atom Newtonian solvated simulations. Hydropathic bioinformatic scaling reveals many wave-like features of strained Hgb structures at the coarse-grained amino acid level, while distinguishing between these features thermodynamically. Strain fields localized near hemes interfere with extended strain fields associated with dimer interfacial misfit, resulting in wave-length dependent dimer correlation function antiresonances.