Expression of Reticulomyxa filosa α- and β-tubulins in Escherichia coli yields soluble and partially correctly folded material

Gene

Volumn 212, Issue 1, 1998, Pages 87-94

  Linder, Stefan ^a   Schliwa, Manfred ^a   Kube Granderath, Eckhard ^a  

^a UNIVERSITY OF MUNICH   (Germany)

Author keywords

Chaperonins; Expression; Folding; Structure; Tubulin

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN;

AMOEBA; ARTICLE; BACTERIUM CULTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SYNTHESIS;

AMOEBA; ANIMALS; BASE SEQUENCE; DNA PRIMERS; ENDOPEPTIDASES; ESCHERICHIA COLI; GENE EXPRESSION; GROEL PROTEIN; GROES PROTEIN; POLYMERASE CHAIN REACTION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SOLUBILITY; TUBULIN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; NEGIBACTERIA; PROKARYOTA; PROTOZOA; RETICULOMYXA FILOSA;

EID: 0032575036     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00142-5     Document Type: Article

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