Tying up the loose ends: Circular permutation decreases the proteolytic susceptibility of recombinant proteins

Protein Engineering, Design and Selection

Volumn 22, Issue 10, 2009, Pages 607-613

  Whitehead, Timothy A ^a   Bergeron, Lisa M ^a   Clark, Douglas S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

lactamase; Chaperone; Circular permutation; Protein engineering; Proteolysis

Indexed keywords

CHAPERONE; CHAPERONIN; CIRCULAR PERMUTATION; DESIGN CRITERION; E. COLI; LACTAMASES; PERIPLASM; PROTEIN ENGINEERING; PROTEOLYTIC SUSCEPTIBILITY; RECOMBINANT PROTEIN; RECOMBINANT PROTEIN EXPRESSION; TEM; WILD TYPES;

BIOCHEMICAL ENGINEERING; ESCHERICHIA COLI; GENETIC ENGINEERING;

PROTEINS;

BETA LACTAMASE TEM 1; CHAPERONIN; RECOMBINANT PROTEIN;

ARTICLE; BACTERIAL STRAIN; CYTOPLASM; ESCHERICHIA COLI; GENETIC ENGINEERING; METHANOCOCCUS JANNASCHII; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN ENGINEERING; PROTEIN EXPRESSION; WILD TYPE;

BETA-LACTAMASES; ESCHERICHIA COLI; KINETICS; MODELS, MOLECULAR; PENICILLIN AMIDASE; PROTEIN ENGINEERING; PROTEIN STABILITY; RECOMBINANT PROTEINS; THERMOSOMES;

ESCHERICHIA COLI; METHANOCALDOCOCCUS JANNASCHII;

EID: 78149378424     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzp034     Document Type: Article

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