Abstract
AbstractThe contribution of solvation energy to guiding molecular recognition for six rigid protein‐peptide systems bad been evaluated by the variation in the number of the identified native‐like configurations and in the driving force of specific interaction resulting from the addition of the explicit solvation term in the force field function. The AMBER force field energy and the total energy including the force field energy and the WZS solvation energy were calculated for sampled configurations. The results obtained by the calculations of both force field and total energies were compared with each other. It suggests that the contribution of solvation energy is important to guiding the specific recognition of the systems in which the ligands possess larger hydrophobic or aromatic residues while the protein receptors provide the active surfaces with hydrophobic property.
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