The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 20, 2005, Pages 7139-7144

  Ramachandran, Rajesh ^a   Tweten, Rodney K ^b   Johnson, Arthur E ^a,c,d  

^a TEXAS A AND M UNIVERSITY   (United States)

^b UNIVERSITY OF OKLAHOMA COLLEGE OF MEDICINE   (United States)

^c TEXAS A AND M HEALTH SCIENCE CENTER   (United States)

^d Department of Neuroscience and Experimental Therapeutics   (United States)

Author keywords

Fluorescence; Membrane; Membrane protein; Toxin

Indexed keywords

BACTERIAL TOXIN; CHOLESTEROL; CLOSTRIDIUM PERFRINGENS TOXIN; CYTOLYSIN; UNCLASSIFIED DRUG;

ARTICLE; CHANNEL GATING; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENERGY TRANSFER; FLUORESCENCE RESONANCE ENERGY TRANSFER; MEMBRANE BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN LOCALIZATION;

BACTERIAL TOXINS; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CYTOTOXINS; FLUORESCENCE POLARIZATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEMOLYSIN PROTEINS; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY;

EID: 18844417932     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0500556102     Document Type: Article

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