Energy Study at Different Temperatures for Active Site of Azurin in Water, Ethanol, Methanol and Gas Phase by Monte Carlo Simulations

The interaction between the solute and the solsent molecules play a crucial role in understanding the various molecular processes involved in chemistry and biochemistry, so in this work the potential energy of active site of azurin have been calculated in solvent by the Monte Carlo simulation. In this paper we present quantitative results of Monte Carlo calculations of potential energies of active site of azurin in water, ethanol, methanol and gas phase at three temperatures 300, 305,310 K. According to the obtained results, the potential energy of active site conformation is decreased quickly in water and the greater stability in this study is related to at.er and then methanol. It has been found that in different solsent media the highest potential energy value and then the least stability correspond to ethanol and also through increasing the dielectric constant of solvent the structural energy values decreased. Thus, the protein environment, which is often aqueous. aftects the structure. folding dynamic and stability, and, therefore, the functionality of globular proteins. In fact, solvent-protein interactions, together with the interactions between residues in the protein matrix, facilitate the folding process and establishment of intermolecular interactions with other complex systems Furthermore, to be properly folded and fully functional, a protein requires a minimum lesel of hydration.