title: The primary structure of the ribosomal protein L29 from Escherichia coli.
abstract: The amino acid sequence of ribosomal protein L29 was determined utilizing an improved Beckman sequenator, a solid phase peptide sequenator, and more conventional techniques. L29 is composed of 63 amino acid residues and has a molecular weight of 7262. It lacks proline, cysteine, isoleucine, tyrosine and tryptophan. The N-terminal and C-terminal regions (residues 1-9 and 50-63) are basic, while the rest of the molecule is hydrophobic and neutral. Calculated P-a values show two helical regions: one from residues 1 through 32 and the other from residues 37 through 47. No beta-sheet regions are predicted. Short identical regions occur within the sequence of L29 as well as between L29 and other ribosomal proteins.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins; D004926:Escherichia coli / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D011487:Protein Conformation; D012270:Ribosomes / Q000032:analysis*; D013210:Staphylococcus / Q000201:enzymology; D013820:Thermolysin; D014357:Trypsin
chemical_list: D000596:Amino Acids; D001426:Bacterial Proteins; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D014357:Trypsin; D013820:Thermolysin