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• W4353013826 abstract "Accurate determination of the thermodynamic and molecular mechanical properties of amino acids will contribute to a better understanding of their folding mechanisms. In this study, the enthalpy values and molecular mechanics parameters of 17 amino acids were investigated by the classical molecular dynamics method. All calculations were performed using the force-field potential approach. As a result, the calculated solid formation enthalpy for ALA, ASN, ASP, CYS, LYS, and PHE are in good agreement with the experimental data. In addition, molecular mechanics parameters such as Coulomb, bond, angle, dihedral, and Van der Waals were calculated for all amino acids. It is seen that the Coulomb energy is quite low compared to the rest of the molecular mechanical energies. The molecular mechanical energies obtained from the study will contribute to protein-lipid modification studies for electronic interaction, ligand binding to the cell surface, and correct protein localization." @default.
• W4353013826 created "2023-03-23" @default.
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• W4353013826 date "2023-03-22" @default.
• W4353013826 modified "2023-09-27" @default.
• W4353013826 title "Investigation of Solid Formation Enthalpy and Molecular Mechanics Energies of Amino Acids via Force Field Approach" @default.
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• W4353013826 doi "https://doi.org/10.17798/bitlisfen.1146682" @default.
• W4353013826 hasPublicationYear "2023" @default.
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