Hemoglobin Strain Field Waves and Allometric Functionality

TL;DR

This paper investigates the wave-like strain fields in hemoglobin structures using bioinformatic scaling and simulations, revealing how strain localization and interference affect hemoglobin's stability and function.

Contribution

It introduces a novel analysis of hemoglobin strain fields at the amino acid level, linking structural waves to thermodynamic properties and functional implications.

Findings

Identification of wave-like features in hemoglobin structures.

Demonstration of strain field interference effects.

Correlation between strain localization and thermodynamic behavior.

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.