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.
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