The solvation model given by Equation 1 and applied here to amino acids can also be used to interpret molecular dynamics results of other small molecules containing the same functional groups, and extended for other functional groups. The model is also directly relevant for proteins: together with short molecular dynamics simulations of proteins in the folded and unfolded ensembles, it can be used to gain insight into how fluorination-induced changes in protein-water interactions contribute to changes in the free energy of folding. Good sampling of the folded protein ensemble can easily be achieved in many cases with molecular dynamics simulations; to sample the un-folded protein ensemble, one can take advantage of a number of algorithms . Future work by our group will attempt to extend the solvation model to include mechanisms by which fluorination alters intra-protein non-bonded interactions. This extension is necessary to obtain a complete picture of the mechanisms by which fluorination alters the thermal stability of proteins.