A theoretical method for the rational design of a "universal" scorpion toxin with a wider spectrum of specificity for K+ channels and a more stable alpha/beta-folding than in its natural homologues is described. On the basis of the analysis of molecular hydrophobic potentials (MHP) of the protein spatial structures, structural features for a family of five short scorpion toxins were revealed. The analysis of the maps of two-dimensional intramolecular MHP contacts allowed the identification of amino acid residues responsible for the folding of the protein and/or for the manifestation of its specific function. The theoretically predicted structure-function roles of the residues were compared with experimental data on the mutagenesis of charybdotoxin. Based on the results of MHP calculations and with the theory of protein molecular evolution used as an additional criterion for the selection of mutations, the amino acid sequence and the spatial structure of a "universal" scorpion toxin were determined.