[Preparation, isolation, and study of mutant forms of ribosomal protein L7/L12]

Abstract

Three mutant forms of the ribosomal protein L7/L12 with Ser1, Met14 and Met26 substituted by the Tyr residue were constructed for studying the 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 proteins' purification were developed. The mutant proteins L7/L12 are very close, in structure and properties to the wild type protein and represent suitable objects for the 1H-NMR study of the N-terminal domain.