Search

Contradictory data in the huge literature on microwaves bio-effects may result from a poor understanding of the mechanisms of interaction between microwaves and biological systems. Molecular simulations of biochemical processes seem to be a promising tool to comprehend microwave induced bio-effects. Molecular simulations of classical and quantum events involved in relevant biochemical processes enable to follow the dynamic evolution of a biochemical reaction in the presence of microwave fields. In this paper, the action of a microwave signal (1 GHz) on the covalent binding process of a ligand (carbon monoxide) to a protein (myoglobin) has been studied. Our results indicate that microwave fields, with intensities much below the atomic/molecular electric interactions, cannot affect such biochemical process. Index Terms--Bioelectromagnetics, microwaves bio-effects, molecular simulations, myoglobin.

The effect of a point mutation on the enzymatic activity of copper-zinc superoxide dismutase CuZn, which was studied by means of a theoretical-computational procedure, was investigated. The data revealed the mechanical-dynamical architecture of the enzyme, altered by an apparently irrelevant mutation, suggesting a possible atomic-molecular-based explanation for the mutant-pathology correlation.

The use of quasi-Gaussian entropy (QGE) theory in treating systems of polyatomic flexible molecules, where the usual semigrid description may not be appropriate shown. The ability of the theory to describe intramolecular energy fluctuations and conformational equilibria of purely classical molecules in the ideal gas condition is also examined.

A method is developed by using an extended quasi-Gaussian entropy theory parameterized via use of molecular dynamics simulation that provides a complete description of the thermodynamics of peptide conformational states. The method is applied to analyze the conformational thermodynamics of MR121-GSGSW, a peptide that possesses the lowest partial molar entropy.

A detailed study was conducted to quantitatively address the thermodynamics of compound 0 (Cpd 0) formation in horseradish peroxidase (HRP) enzyme. The results data obtained provide insight into significant role of specific residues in the reaction pocket and the conformational fluctuations of the overall environment in physiological conditions.

The first step of the copper-zinc superoxide dismutase enzymatic cycle, involving the binding of a superoxide anion, and the simultaneous detachment of His63 is investigated. Results show that the protein-solvent environment fluctuations are essential to understand the reaction mechanism, which is based on the concerted rupture of the copper-histidine coordination bond and the copper-superoxide bond in the active site.

The electronic properties of peridinin are investigated. Density functional theory with a time dependent treatment is used for this purpose.

The framework of the quasi-Gaussian entropy (QGE) theory was used to formulate a general model for the description of the thermodynamic properties of the folding/unfolding of single-domain proteins. This theory provides models for homogeneous fluids, solids, and recently for the thermodynamics of flexible organic molecules in vacuo and solutes.

Molecular dynamics simulations are combined with the quasi-Gaussian entropy (QGE) theory to model the statistical mechanics and the thermodynamics of ionic solutions. Results showed that the use of the gamma state model provides an excellent theoretical description of the solution behavior over a wide range of temperature.