Secondary structure forming propensity coupled with amphiphilicity is an optimal motif in a peptide or protein for association with chaperonin 60 (GroEL)

Biochemistry

Volumn 38, Issue 32, 1999, Pages 10272-10286

  Preuss, Monika ^a   Hutchinson, Jonathan P ^a,b   Miller, Andrew D ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

^b NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; DANSYL CHLORIDE; PEPTIDE;

ARTICLE; FLUORESCENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE;

BINDING, COMPETITIVE; CHAPERONIN 60; CIRCULAR DICHROISM; ESCHERICHIA COLI; GROEL PROTEIN; GROES PROTEIN; MODELS, MOLECULAR; MOLECULAR MIMICRY; PEPTIDES; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

EID: 0033543136     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi990342l     Document Type: Article

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