Comparison of the conformation, hydrophobicity, and model membrane interactions of diphtheria toxin to those of formaldehyde-treated toxin (diphtheria toxoid): Formaldehyde stabilization of the native conformation inhibits changes that allow membrane insertion

Biochemistry

Volumn 35, Issue 7, 1996, Pages 2374-2379

  Paliwal, Ranjana ^a   London, Erwin ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIPHTHERIA TOXIN; DIPHTHERIA TOXOID; DIPHTHERIA VACCINE; FORMALDEHYDE;

ARTICLE; CORYNEBACTERIUM DIPHTHERIAE; DIPHTHERIA; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN STABILITY; TOXIN ANALYSIS; VACCINE PRODUCTION;

BINDING SITES; DIPHTHERIA TOXIN; DIPHTHERIA TOXOID; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FORMALDEHYDE; GUANIDINE; GUANIDINES; HEAT; MEMBRANES, ARTIFICIAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE;

EID: 0030030017     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952469q     Document Type: Review

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