CONSTRUCTION, PURIFICATION AND STUDY OF THE PROTEIN L7 L12 MUTANT FORMS/

Three mutant forms of the ribosomal protein L7/L12 with Ser1, Met14 an d Met26 substituted by the Tyr residue were constructed for studying t he protein's N-terminal domain. Three point mutations were introduced into the L7/L12 gene by means of the phage M13mp18 system, the mutant genes were expressed in Escherichia coli cells, and methods of the pro teins' purification were developed. The mutant proteins L7/L12 are ver y close, in structure and properties to the wild type protein and repr esent suitable objects for the H-1-NMR study of the N-terminal domain.