Location of tryptophan residues in free and membrane bound Escherichia coli α-hemolysin and their role on the lytic membrane properties

Biochimica et Biophysica Acta - Biomembranes

Volumn 1464, Issue 1, 2000, Pages 27-34

  Verza, Georgina ^a   Bakás, Laura ^a,b  

^a Facultad de Ciencias Naturales e Instituto M Lillo   (Argentina)

^b FACULTAD DE CIENCIAS EXACTAS   (Argentina)

Author keywords

Hemolysin; Chemical modification; Lytic toxin; Protein membrane interaction; Tryptophan fluorescence

Indexed keywords

HEMOLYSIN; N BROMOSUCCINIMIDE; TRYPTOPHAN;

ARTICLE; CHEMICAL MODIFICATION; CYTOLYSIS; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; LIPID BILAYER; LYSIS; MEMBRANE BINDING; NONHUMAN; OXIDATION; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; TOXIN STRUCTURE;

BACTERIAL PROTEINS; BACTERIAL TOXINS; BROMOSUCCINIMIDE; CELL MEMBRANE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEMOLYSIN PROTEINS; LIPID BILAYERS; OXIDATION-REDUCTION; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

ESCHERICHIA COLI; EUKARYOTA;

EID: 0033975633     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(99)00244-8     Document Type: Article

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