Design, NMR characterization and activity of a 21-residue peptide fragment of bacteriocin AS-48 containing its putative membrane interacting region

Journal of Peptide Science

Volumn 11, Issue 1, 2005, Pages 29-36

  Angeles Jimenez M ^a   Barrachi Saccilotto, Ana C ^a   Valdivia, Eva ^b   Maqueda, Mercedes ^b   Rico, Manuel ^a  

^a INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^b UNIVERSITY OF GRANADA   (Spain)

Author keywords

13C NMR; 1H NMR; Antimicrobial activity; Peptide structure

Indexed keywords

ANTIBIOTIC AGENT; BACTERIOCIN AS 48; HELIX LOOP HELIX PROTEIN; POLYPEPTIDE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANTIMICROBIAL ACTIVITY; AQUEOUS SOLUTION; ARTICLE; BACTERIAL CELL; BACTERIAL MEMBRANE; CARBON NUCLEAR MAGNETIC RESONANCE; CONFORMATIONAL TRANSITION; DRUG STRUCTURE; DRUG SYNTHESIS; ELECTROSTATIC PRECIPITATION; ENTEROCOCCUS FAECALIS; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; HYDROPHOBICITY; LISTERIA MONOCYTOGENES; MEMBRANE PERMEABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

BACTERIOCINS; CELL MEMBRANE; HELIX-TURN-HELIX MOTIFS; LISTERIA MONOCYTOGENES; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE FRAGMENTS;

BACTERIA (MICROORGANISMS); ENTEROCOCCUS; ENTEROCOCCUS FAECALIS; NEGIBACTERIA; POSIBACTERIA;

EID: 11944271727     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.589     Document Type: Article

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