Molecular mechanic calculations and evaluation the impacts of salvation on environmental and thermodynamic effects of enzyme choline acetyltransferase

Abstract Cholinergic neurons play an important role in muscle contraction، in learning and memory. Choline acetyltransferase is the enzyme that is responsible for the synthesis of acetylcholine and is a specific marker for choiinergic neurons. Computational methods investigate on Choline acetyltransferase enzyme. The aim of the present work was to describe and characterize the molecular structure vibrational properties of choline acetyltransferase crystalline-structure. In this work، the structures of a coordination compound modeling the choline acetyltransferase computationally. Thus، it is worthwhile to collect information on their structures by the means of computational chemistry as well. Monte Carlo simulations are based on pair wise additive potentials of the form. In concepts and algorithms of classical MD simulations the atoms of a biopolymer move according to the Newtonian equations of motion. These studies provided insights into the steric، electrostatic، hydrophobic، and hydrogen bonding properties and other structural features influencing the choline acetyltransferasewas Potential energies for the three force fields of MM+، AMBER and OPLS at Monte Carlo simulation were compared. Geometry of optimized variables of Bond length (B)، Bond Angle (A) and Dihedral Angle (D) investigated. The potential energy (kcal/mol) via time (ps) during Molecular Dynamic (MD) simulation at300 K in gas (R2 = 0. 7656) and water (R2 = 0. 9794) environments studied to stabilized structure of choline acetyltransferase accepted. These results also were revealed that the solvation of Choline acetyltransferase molecule is the major component for the interaction potential energy and it was clearly shown that the role of the solute-solvent interactions is more pronounced in Choline acetyltransferase molecule and it’s active site solvation.