[Stereochemical theory of the 3-dimensional structure of globular proteins. III. Prediction of the tertiary structure].

A prediction is made of the tertiary structure of parvalbumin, the variable part of the immunoglobulin molecule, carboxypeptidase and the trypsin inhibitor. The structures obtained theoretically coincide completely with the native ones. In the case of the trypsin inhibitor molecule, the theoretical sequence of disulfide bridge formation completely coincides with the experimental data. Elements of symmetry were found in highly helical intermediate structures of the four proteins studied. The theory developed can be successfully applied for assembling the quaternary protein structure. Proceeding from this theory the mechanisms of the increased rate of assembly of protein spatial structure in conditions in vivo as compared with their assembly in vitro are analysed.