Hemoglobin Strain Field Waves and Allometric Functionality
arXiv:1606.00795
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.
10 pages, 4 figures