Abstract
Structural and dynamical behaviors of enzyme are critical for determining its catalytic activity. Knowing that the enzyme activity may vary with different solvent polarity due to the changes in enzyme structure and flexibility, Subtilisin Carlsberg enzyme was subjected to investigate the structural variation upon different solvent systems by using molecular dynamics simulation with explicit solvents. Characterization of the structure and activity focusing on the hydration of the active site will be discussed with the effects of crystallographic water bound to the active site of this enzyme and with the solvent effects.
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