Department of

Computational Biological Chemistry

Biomolecular Solvation

Our focus is on the protein solvation by hydrated ionic liquids for a diversity of mole fractions or ionic strengths.

The systems are analyzed at four levels of resolution:
First, properties representative for the entire protein like the protein-solvent interface surface, the energy, or the root mean squared deviation and fluctuation, are interpreted. Second, the first solvation shell of the protein was characterized in terms of coordination numbers and mean residence times. Third, certain regions of the protein were tracked down to be responsible for the characteristic features found at the two previous levels. Fourth, the characterization of the whole system and its components was done at the mesoscopic level: The atomistic charge distributions were replaced by a dielectric polarization.

Considering the above mentioned properties as a function of the mole fraction or ionic strength two characteristic transition points can be figured out. The first one refers to the transition from the pure aqueous system to the ionic solution. The second characteristic point, corresponds to the transition from the ionic solution to the hydrated ionic melt.


Imprint: (as stipulated by Austrian law, MedienG 2005): S. Boresch / C. Schröder,
Institut für Computergestützte Biologische Chemie, Währinger Strasse 17, 1090 Wien, Austria