Recent work on the protein Actophorin from the amoeba Acanthamoeba castellani identified a series of site directed mutations that increase the thermal stability of the protein by 22 ºC.  Here, we expand this observation by showing that the mutant protein is also significantly stable to both equilibrium and kinetic chemical denaturation, and employ computer simulations to account for the increase in thermal or chemical stability through an accounting of atomic-level interactions. 
THERM