The role of salt bridges in protein protein binding is largely determined by the costs of desolvating the oppositely charged members of the salt bridge upon binding. On the basis of Poisson Boltzmann (PB) implicit solvent calculations, it has been proposed that the reduced desolvation penalties of salt bridges at high temperatures provide one explanation for the increased abundance of salt bridges in hyperthermophilic proteins. Here, for the first time, we directly compare the PB implicit solvent model with several explicit water models in computing the effects of extremely high temperature (i.e., 100 degrees C) on the desolvation penalties of salt bridges across protein protein interfaces. With the exception of two outliers, the desolvation costs at 100 degrees C from implicit and explicit solvent calculations are of similar magnitudes and significantly reduced relative to 25 degrees C. The two outliers correspond to salt bridges that are both buried and part of a salt bridge network, a challenging case that should be considered in the development of fast solvation models.