title: Primary structure of the chromosomal protein HMb from the archaebacteria Methanosarcina barkeri.
abstract: The amino acid sequence of the protein HMb, a protein of 93 residues (Mr 10757) which represents the major acid-soluble component of the Methanosarcina barkeri nucleoprotein complex, has been established from automated sequence analysis of the protein and from structural data provided by peptides derived from cleavage of the protein at aspartic acid, arginine and methionine residues. The protein HMb is mainly characterized by a high amount of charged residues (15% of acidic residues and 26.8% of basic residues) which are distributed all along the polypeptide chain. The amino acid sequence of the protein HMb is not homologous to any eubacterial, archaebacterial or eukaryotic chromosomal proteins known up to now.
mesh_terms: D000595:Amino Acid Sequence; D001105:Archaea / Q000032:analysis*; D019843:Archaeal Proteins; D001419:Bacteria / Q000032:analysis*; D001426:Bacterial Proteins; D055598:Chemical Phenomena; D002621:Chemistry; D010446:Peptide Fragments / Q000032:analysis; D012261:Ribonucleoproteins; D009626:Terminology as Topic
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; C051211:HMb protein, Methanosarcina; D010446:Peptide Fragments; D012261:Ribonucleoproteins