The ß-chain of the HHB protein's molecular dynamics (MD) simulation showing truncated octahedron boundary explicit water solvated and hydrogen atoms in color.

<p>The MD simulations system used in calculations are; <b>a</b>) water box without the protein, <b>b</b>) water box surrounding the entire protein (middle) and <b>c</b>) tertiary structure of the wild type <i>ß</i>-chain of HHB protein showing disease causing mutations i.e. green <i>HbE</i>26 Glu→Lys (E→K), orange <i>HbD</i>121 Glu→Gln (E→Q), blue <i>HbC</i>6 Glu→Lys (E→K) and <i>HbS</i>6 Glu→Val (E→V) on 3 helixes using predict mesh modeling. The visual inspection also allow to identify the side chain of a histidine residue involved in the hydrogen bonding with surrounding molecules and in that case the δ nitrogen of the histidine (HSB) is protonated residue.