Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli.
摘要：
Describes the selection of mutations in Escherichia coli that allow disulfide bond formation in the cytoplasm. Importance of disulfide bonds in the folding and structure of proteins; Absence of necessity of Thioredoxin for disulfide bond formation; Implication of thioredoxin reductase in keeping cysteines reduced in cytoplasmic proteins.
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关键词：
Cytoplasm Escherichia coli Disulfides Cysteine Alkaline Phosphatase Protein Sorting Signals Recombinant Proteins Protein Folding Oxidation-Reduction Mutation
DOI：
10.1126/science.8259521
被引量：
年份：
1993
万方医学
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