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Hemoglobin exhibits allosteric structural changes upon ligand binding due tothe dynamic interactions between the ligand binding sites, the amino acidsresidues and some other solutes present under physiological conditions. In thepresent study, the dynamical and quaternary structural changes occurring in twounligated (deoxy-) T structures, and two fully ligated (oxy-) R, R2 structuresof adult human hemoglobin were investigated with molecular dynamics. It isshown that, in the sub-microsecond time scale, there is no marked difference inthe global dynamics of the amino acids residues in both the oxy- and the deoxy-forms of the individual structures. In addition, the R, R2 are relativelystable and do not present quaternary conformational changes within the timescale of our simulations while the T structure is dynamically more flexible andexhibited the T\rightarrow R quaternary conformational transition, which ispropagated by the relative rotation of the residues at the {\alpha}1{\beta}2and {\alpha}2{\beta}1 interface.

Role of the Subunits Interactions in the Conformational Transitions in Adult Human Hemoglobin: an Explicit Solvent Molecular Dynamics Study