Low folding propensity and high translation efficiency distinguish in vivo substrates of GroEL from other Escherichia coli proteins

Bioinformatics

Volumn 23, Issue 24, 2007, Pages 3276-3279

  Noivirt Brik, Orly ^a   Unger, Ron ^b   Horovitz, Amnon ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b BAR ILAN UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; ESCHERICHIA COLI PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CONCEPTUAL FRAMEWORK; ESCHERICHIA COLI; IN VIVO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SYNTHESIS; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURAL BIOINFORMATICS; TRANSLATION REGULATION; UREAPLASMA UREALYTICUM;

ESCHERICHIA COLI; UREAPLASMA UREALYTICUM;

EID: 36949006280     PISSN: 13674803     EISSN: 13674811     Source Type: Journal    
DOI: 10.1093/bioinformatics/btm513     Document Type: Article

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