  The hydrophobic effect stabilizes the native structure of proteins by
minimizing the unfavourable interactions between hydrophobic residues and water
through the formation of a hydrophobic core. Here we include the entropic and
enthalpic contributions of the hydrophobic effect explicitly in an implicit
solvent model. This allows us to capture two important effects: a length-scale
dependence and a temperature dependence for the solvation of a hydrophobic
particle. This consistent treatment of the hydrophobic effect explains cold
denaturation and heat capacity measurements of solvated proteins.
