Theoretical prediction on functional domains from the primary structure of enterotoxin B and correlation with experimental data.

Theoretical analysis of the primary amino acid structure of St. aureus enterotoxin B for predicting some structure-functional characteristics is presented. The method is based on correlation between the spectrum of numerical presentation of any amino acid sequence and its biological function. This is accomplished by assigning to each amino acid a numerical value. The mathematical processing of the data is carried out with a digital robust algorithm on the basis of running media and mean filtering. The above analysis indicates that SEB contains in the polypeptide chain at least some abnormal regions whose correlation with our experimental data is shown. Three of these have a stable conformation, while the other seven domains may be formed upon an additional energy action on the molecule, which indicates the reactive ability of SEB.