The primary structure of the 5s rRNA binding protein L25 of Escherichia coli ribosomes.
The primary structure of protein L25 from the large subunit of Escherichia coli ribosomes was determined by isolation and analysis of peptides obtained after cleavage of the protein with trypsin, thermolysin and Staphylococcus protease as well as by Edman degradation of the intact protein and of a CNBr peptide. The complete amino acid sequence is shown in Fig. 4. There are sequence homologies within protein L25 (Table 6) as well as between protein L25 and other ribosomal proteins (Table 5).
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D004926:Escherichia coli / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins / Q000032:analysis*; D012270:Ribosomes / Q000032:analysis*; D013820:Thermolysin; D014357:Trypsin
D000596:Amino Acids; D010446:Peptide Fragments; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; D014357:Trypsin; D013820:Thermolysin