[The rational evolution of scorpion toxins].

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.