  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.
