Abstract
There has been considerable interest in the physical basis for the increased thermostability of thermophilic proteins with respect to their mesophilic counterparts since the discovery of highly thermo-tolerant organisms. We have systematically studied a large set of protein structures in order to find those properties with the most power to discriminate mesophilic proteins from their thermophilic orthologs. Most of the structure-based descriptors used in our discrimination and classification experiments were derived from the Delaunay tessellations of the protein structures.