Productive interaction of chaperones with substrate protein domains allows correct folding of the downstream GFP domain

Gene

Volumn 350, Issue 1, 2005, Pages 25-31

  Zhang, Aihua ^a   Cantor, Eric J ^a   Barshevsky, Tanya ^a   Chong, Shaorong ^a  

^a NEW ENGLAND BIOLABS   (United States)

Author keywords

Aggregation; Mini intein; Protein folding

Indexed keywords

CHAPERONE; GREEN FLUORESCENT PROTEIN; POLYPEPTIDE;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CROSS COUPLING REACTION; DOWN REGULATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; FLUORESCENCE ANALYSIS; MOLECULAR BIOLOGY; MOLECULAR INTERACTION; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN SECRETION; PROTEIN SYNTHESIS; SOLUBILIZATION; STATISTICAL SIGNIFICANCE; UPREGULATION;

EID: 17044366213     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2005.01.019     Document Type: Article

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