N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers

Protein Science

Volumn 16, Issue 4, 2007, Pages 635-643

  Chul, Woo Kim ^a   Kyoung, Sim Han ^a   Ryu, Ki Sun ^a   Byung, Hee Kim ^a   Kim, Kyun Hwan ^b   Seong, Il Choi ^a   Seong, Baik L ^a  

^a Yonsei University   (South Korea)

^b Konkuk University School of Medicine   (South Korea)

Author keywords

Charge; De novo folding; Fusion; Multidomain proteins; N terminal domains; Size; Solubility enhancers

Indexed keywords

ACONITATE HYDRATASE; HYBRID PROTEIN; LYSINE TRANSFER RNA LIGASE; THREONINE TRANSFER RNA LIGASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ESCHERICHIA COLI; IN VIVO STUDY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN TARGETING; WESTERN BLOTTING;

ACONITATE HYDRATASE; BLOTTING, WESTERN; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI PROTEINS; LYSINE-TRNA LIGASE; MODELS, MOLECULAR; PROTEIN FOLDING; SOLUBILITY; TANDEM REPEAT SEQUENCES; THREONINE-TRNA LIGASE;

EID: 33947728505     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062330907     Document Type: Article

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