Model peptide studies demonstrate that amphipathic secondary structures can be recognized by the chaperonin GroEL (cpn60)

Journal of Biological Chemistry

Volumn 272, Issue 8, 1997, Pages 5105-5111

  Brazil, Bill T ^a   Cleland, Jeffrey L ^b   McDowell, Robert S ^b   Skelton, Nicholas J ^b   Paris, Ken ^b   Horowitz, Paul M ^a  

^a UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

^b GENENTECH INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APAMIN; BEE VENOM; CHAPERONIN; HYBRID PROTEIN; THIOSULFATE SULFURTRANSFERASE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; DISSOCIATION CONSTANT; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; CHAPERONIN 60; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 0031046191     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.8.5105     Document Type: Article

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