engleski

Modelling Structural Properties of Copper(II) Amino Acid Complexes in Different Environments

In living organisms low-molecular-weight essential transition metal complexes with amino acids, peptides, and proteins are supposed to be a part of exchangeable pool for the transition metal storage and transport for most tissues. Most spectroscopic and electrochemical methods cannot give complete information on the geometry of the metal-bioligand complexes in solutions especially if the number of ligand binding sites is larger then 2, and the exact geometries of such complexes are still elusive. The structural properties can be predicted and reproduced with theoretical molecular modelling methods. To reliably predict properties in solution using MD method, it is necessary to use a reliable MM force field. We develop reliable force fields without incorporating the environmental effects into the empirical parameters but the effects are explicitly accounted [1-4]. Hence, we calculate equilibrium molecular geometry of copper(II) amino acid complexes in vacuo and in the condensed phase using the same set of potential energy functions and empirical parameters [2-6]. This paper presents the applications of the force fields to examine the effects of intermolecular interactions (crystal lattice effects, hydrogen bonding in crystal and in solution) on the molecular geometry of the copper(II) amino acid complexes.

molecular mechanics; force field; vacuum structure; crystal structure; simulation; molecular dynamics; copper; amino acid

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