European Journal of Biochemistry · 1986 · 20 citations · 16 references
Life SciencesBiochemistryMicrobiologyProtein BiochemistryProtein Structure PredictionStructural BiologyAmino Acid Sequence DeterminantsAmino Acid StructureProtein CharacterizationProtein Sequence AnalysisProtein StructureAmino Acid Composition AnalysisAmino Acid Sequence-structure Relationships
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.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
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Polyquarternary amines prevent peptide loss from sequenators
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R J DeLange, D M Fambrough, Emil L. Smith et al. · Journal of Biological Chemistry · 1969 · 451 citations · Full text