  We implement a well-established concept to consider dispersion effects within
a Poisson-Boltzmann approach of continuum solvation of proteins. The
theoretical framework is particularly suited for boundary element methods. Free
parameters are determined by comparison to experimental data as well as
high-level quantum mechanical reference calculations. The method is general and
can be easily extended in several directions. The model is tested on various
chemical substances and found to yield good-quality estimates of the solvation
free energy without obvious indication of any introduced bias. Once optimized,
the model is applied to a series of proteins, and factors such as protein size
or partial charge assignments are studied.
