Abstract
We have investigated additional effect of protein denaturant agent (guanidine hydrochloride (GdnHCl)) on the hydrophobic hydration structure in the aqueous protein model (n-tetrapropylammonium chrolide (n-Pr_4NCl)) solution at 77K as a function of GdnHCl concentration. It is found that the addition of GdnHCl induces the disruption of the hydration structure in the aqueous n-Pr_4NCl solution. We suggest that the hydrophobic interaction changes to other interactions such as n-Pr_4N^+H…H_2O or n-Pr_4N^+…GdnHCl by the addition of GdnHCl.
