  We elucidate the mechanism of cold denaturation through constant-pressure
simulations for a model of hydrophobic molecules in an explicit solvent. We
find that the temperature dependence of the hydrophobic effect is the driving
force/induces/facilitates cold denaturation. The physical mechanism underlying
this phenomenon is identified as the destabilization of hydrophobic contact in
favor of solvent separated configurations, the same mechanism seen in pressure
induced denaturation. A phenomenological explanation proposed for the mechanism
is suggested as being responsible for cold denaturation in real proteins.
