[New criteria in the inverse problem of protein structure formation]

New approach to the inverse protein folding problem has been developed. It is helpful for search amino acid sequences of proteins having certain tertiary structure. Also it looks for the best three dimensional structure among known ones for a given amino acid sequence. We introduced new parameters for delineating geometry and physical properties of protein tertiary structure and new evaluation function to distinguish between correct fold and large number of misfolds. The method can be used for checking de novo constructed proteins and for creating enlarged bank of three dimensional protein structures on the basis of known primary protein structures.