Rational design of translational pausing without altering the amino acid sequence dramatically promotes soluble protein expression: A strategic demonstration

Journal of Biotechnology

Volumn 189, Issue , 2014, Pages 104-113

  Chen, Wei ^a   Jin, Jingjie ^a   Gu, Wei ^a   Wei, Bo ^a   Lei, Yun ^a   Xiong, Sheng ^a   Zhang, Gong ^a  

^a JINAN UNIVERSITY   (China)

Author keywords

Antiviral activity; Cyanovirin N; Escherichia coli; Protein folding; Synonymous substitutions; Translation pausing

Indexed keywords

PROTEIN FOLDING;

AMINO ACID SEQUENCE; ANTIVIRAL ACTIVITIES; RATIONAL DESIGN; SOLUBLE PROTEINS; SYNONYMOUS SUBSTITUTIONS;

ESCHERICHIA COLI;

CYANOVIRIN N; RECOMBINANT PROTEIN; RECOMBINANT PROTEINS;

AMINO ACID SEQUENCE; ANTIVIRAL ACTIVITY; ARTICLE; CODING; COMPUTER MODEL; ESCHERICHIA COLI; GENE MUTATION; HETEROLOGOUS EXPRESSION; HUMAN; HUMAN CELL; NUCLEOTIDE SEQUENCE; PROTEIN EXPRESSION; PROTEIN FOLDING; WILD TYPE; CHEMISTRY; METABOLISM; PROTEIN BIOSYNTHESIS;

AMINO ACID SEQUENCE; ESCHERICHIA COLI; PROTEIN BIOSYNTHESIS; PROTEIN FOLDING; RECOMBINANT PROTEINS;

EID: 84908327660     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.08.031     Document Type: Article

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