In this study, the dynamics structures of the enzyme in aqueous solution at 300 Kelvin and 310.5 Kelvin were obtained. The results indicate that the average structure of the human apo-enzyme from this study is comparable to the binary complex obtained from X-ray and nuclear magnetic resonance techniques studied at 298 Kelvin. Slight expansion of the protein, the changes of the secondary structure elements, the disruption of hydrogen bonds and the formation of the new ones for some segments could be observed by taking the X-ray and the nuclear magnetic resonance studies of the binary enzyme-ligands, folate and methotrexate, complexes into consideration together with this study. Furthermore, comparisons of the simulated dynamics structures between the two different temperatures show their structural similarity in terms of the regular secondary structure and overall folding of the protein.
