Investigation Hardness, Enthalpy of Formation analysis of Magnesium Ion Bonded Dimers of Substituted Amino Acids: A DFT Study

Magnesium is an essential element in biological systems. It occurs typically as the Mg2+ ion. For example, ATP (Adenosine triphosphate), the main source of energy in cells, [1]. For the understanding the mechanism of magnesium ion activity in biological system functions, it is necessary to study the interaction of magnesium ion with protein chain[2,3]. Interaction of magnesium ion with simple system such as amino acids may be considered as estimation of interaction of metal ion with protein. In this research the structure and properties of magnesium ion bonded to the different substituted amino acids were calculate by middle tentative methods. In this research structure of amino acids, complex of Magnesium with amino acids and Magnesium ion bonded dimer of them were calculated by DFT methods and 6-311++g** basis set. Analysis of energy parameters of all species were done to calculate the enthalpy of formation of Magnesium ion bonded dimer. Finally Ƞ of the Magnesium ion bonded dimer were calculated. The results shows that if one substitution release the electron to reduce the positive charge on Magnesium ion, will strengthen the Mg2+ ion to oxygen and will increase the enthalpy of formation of dimers. The Ƞ of Magnesium ion in each dimer was calculated and the results show the increase in hardness on Magnesium ion with increase in positive charge on it [4].

Keywords:

Magnesium Ion , ATP , Amino acids , Interaction , DFT