GroEL recognizes an amphipathic helix and binds to the hydrophobic side

Journal of Biological Chemistry

Volumn 284, Issue 7, 2009, Pages 4324-4331

  Li, Yali ^a   Gao, Xinfeng ^a   Chen, Lingling ^a,b  

^a INDIANA UNIVERSITY   (United States)

^b IndianaUniversity ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPATHIC; AMPHIPATHIC STRUCTURE; APICAL DOMAIN; FLUORESCENCE QUENCHING; HELICAL CONFORMATION; HYDROPHOBIC SURFACES; MOLECULAR CHAPERON; NATIVE FORMS; NMR STUDIES; NON-NATIVE; PEPTIDE COMPLEX; PEPTIDE-BINDING; PHAGE DISPLAY; STRUCTURAL MOTIFS; STRUCTURAL STUDIES; SUBSTRATE PROTEINS; SUBSTRATE-BINDING SITES; WORK SUPPORT;

AMINES; BINDING ENERGY; BINDING SITES; CONFORMATIONS; ESCHERICHIA COLI; HYDROPHOBICITY; PROTEIN FOLDING; QUENCHING; SURFACE CHEMISTRY;

SUBSTRATES;

CHAPERONIN; ADENOSINE TRIPHOSPHATE; ESCHERICHIA COLI PROTEIN;

ALPHA HELIX; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HYDROPHOBICITY; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; CHEMISTRY; ESCHERICHIA COLI; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PEPTIDE MAPPING; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE;

ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GROEL PROTEIN; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE MAPPING; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 63249121483     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M804818200     Document Type: Article

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