Etude théorique de la solvatation d'acides aminés avec un modèle minimaliste

Abstract : The hydrophobic effect is one of the major forces that govern protein folding. We study the hydrophobic effect thermodynamical origins towards the transfer into solution of apolar amino acids and of polar amino acids.Their solvation mechanisms are compared with respect to the temperature. The amino acids and the solvent are represented by a coarse grain model in two dimensions. Monte Carlo simulations in the isothermal isobaric ensemble are performed to compute the thermodynamics of transfer of the amino acids and of homologue compounds of their side chains. There is a good qualitative agreement between the experimental data of the solvation free energy of the side chains and their computed values with the model using thermodynamic integration.The study of thermodynamics of transfer gives insight into the importance of the enthalpic and the entropic contributions to the solvation free energy. Two dimensional distribution maps of water molecules are computed around a polar amino acid, the glutamine, and around an apolar amino acid, the isoleucine, with respect to their hydrogen bonds numbers. These maps show the solvent structure in the vicinity of the solutes. The major transfer thermodynamics differences can be explained by the different impacts of the solutes on the solvent structure.
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Jean-Paul Becker. Etude théorique de la solvatation d'acides aminés avec un modèle minimaliste. Autre. Université Henri Poincaré - Nancy 1, 2006. Français. ⟨NNT : 2006NAN10098⟩. ⟨tel-01754316⟩

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