[Preparation, isolation, and study of mutant forms of ribosomal protein L7/L12].
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.
Todorova
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D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D009682:Magnetic Resonance Spectroscopy; D010957:Plasmids; D017354:Point Mutation; D012269:Ribosomal Proteins / Q000235:genetics / Q000302:isolation & purification*
D029968:Escherichia coli Proteins; D012269:Ribosomal Proteins; C512844:rplL protein, E coli; C016700:ribosomal protein L7-L12
Poluchenie, vydelenie i issledovanie mutantnykh form ribosomnogo belka L7/L12.