Abstract
The effect of trehalose on the activity and structural change of lysozyme induced by the chemical denaturant guanidinium chloride (GdmCl) has been investigated using the activity assay, spectroscopy as well as molecular dynamics simulation methods. The activity along with secondary and tertiary content of lysozyme decreases drastically in the presence of GdmCl whereas the addition of trehalose in GdmCl reverses the effect. It has been observed that the addition of trehalose in GdmCl affects mainly to the active site of lysozyme unlike the case of urea in which water gets accommodate at the surface of the protein. This study suggests that addition of trehalose in GdmCl changes the solvent environment more like to the native condition in the active site of lysozyme and modifies the electrostatic and Lennard-Jones interactions which play an important role in the reversal of its activity as well as structural change.
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