Solvation thermodynamics data are essential in the characterization and interpretation of any process carried out in the liquid phase. The data have application in the study of biochemical processes such as protein folding and protein-protein association in aqueous fluids and are useful as benchmarks against which future experimental determinations and theoretical predictions may be compared.
The goal of this research is to provide a consistent, high-quality compilation of solvation thermodynamics data for a set of pure fluids. This is accomplished by using the standard definition of the solvation process to permit solvation thermodynamic quantities to be derived from the fluid property data obtained from REFPROP.
The previous results are currently being updated to be consistent with the latest REFPROP 9.0 models, and will be published in a suitable journal.