title: The complete amino acid sequences of ribosomal proteins L17, L27, and S9 from Bacillus stearothermophilus.
abstract: The complete primary structures of proteins L17, L27 and S9 extracted from the Bacillus stearothermophilus ribosomes with 1 M NaCl and purified to homogeneity by column chromatography have been determined. The amino acid sequences of these proteins are compared to those of the homologous ribosomal proteins from Escherichia coli. The number of identical amino acid residues between the homologous proteins lies between 33-55%.
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000032:analysis; D001411:Geobacillus stearothermophilus / Q000032:analysis*; D011487:Protein Conformation; D000091243:Ribosomal Protein S9; D012269:Ribosomal Proteins / Q000302:isolation & purification*
chemical_list: D001426:Bacterial Proteins; D000091243:Ribosomal Protein S9; D012269:Ribosomal Proteins; C032493:ribosomal protein L17; C034661:ribosomal proteins L27