Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity

European Journal of Biochemistry

Volumn 269, Issue 24, 2002, Pages 6212-6222

  Blond, Alain ^a   Cheminant, Michel ^a   Destoumieux Garzón, Delphine ^a   Ségalas Milazzo, Isabelle ^b   Peduzzi, Jean ^a   Goulard, Christophe ^a   Rebuffat, Sylvie ^a  

^a MUSÉUM NATIONAL D'HISTOIRE NATURELLE   (France)

^b UNIVERSITÉ DE ROUEN   (France)

Author keywords

Antimicrobial peptide; Conformational stability; Microcin; Molecular modeling; Solution structure

Indexed keywords

ANTIBIOTIC AGENT; MICROCIN J25; PEPTIDE; THERMOLYSIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANTIMICROBIAL ACTIVITY; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; DNA FLANKING REGION; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; SALMONELLA ENTERITIDIS;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; BACTERIOCINS; CIRCULAR DICHROISM; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE BIOSYNTHESIS; PEPTIDES; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; THERMOLYSIN;

ENTERITIDIS; ENTEROBACTERIACEAE; ESCHERICHIA COLI; SALMONELLA ENTERITIDIS;

EID: 0036449410     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03340.x     Document Type: Article

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