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.
@article{arxiv.1606.00795,
title = {Hemoglobin Strain Field Waves and Allometric Functionality},
author = {Vedant Sachdeva and J. C. Phillips},
journal= {arXiv preprint arXiv:1606.00795},
year = {2016}
}