Isopeptide linkage between N-alpha-monomethylalanine and lysine in ribosomal protein S11 from Escherichia coli.
Proc Natl Acad Sci U S A, 1977/11;74(11):4905-8.
PMID: 337304
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Abstract
Protein S11 from the Escherichia coli ribosome has a unique NH2-terminal structure not previously observed among ribosomal proteins. Owing to the formation of an isopeptide bond between a secondary amino acid (N-alpha-monomethylalanine) and the epsilon-amino group of the NH2-terminal lysine residue, a "branching point" is formed. Therefore, two amino acids are seen when the NH2 terminus of the protein is determined.
MeSH terms
Alanine; Amino Acid Sequence; Bacterial Proteins; Chemical Phenomena; Chemistry; Escherichia coli; Hydrolysis; Leucyl Aminopeptidase; Lysine; Oligopeptides; Ribosomal Proteins; Trypsin
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