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Solvation is essential for protein activities. To study internal solvation ofprotein, site-directed mutagenesis is applied. Intrinsic fluorescent probe,tryptophan, is inserted into desired position inside protein molecule forultrafast spectroscopic study. Here we review this unique method for proteindynamics researches. We introduce the frontiers of protein solvation,site-directed mutagenesis, protein stability and characteristics, and thespectroscopic methods. Then we present time-resolved spectroscopic dynamics ofsolvation dynamics inside caves of active sites. The studies are carried out ona globular protein, staphylococcal nuclease. The solvation at internal sites ofthe caves indicate clear characteristics of local environment. These solvationbehaviors correlated to the enzyme activity directly.

Ultrafast solvation dynamics at internal site of staphylococcal nuclease investigated by site-directed mutagenesis