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Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
Under physiological conditions, the Escherichia coli cytoplasm is maintained in a reduced state that strongly disfavors the formation of stable disulfide bonds in proteins. However, mutants in which the reduction of both thioredoxins and glutathione is impaired (trxB gor mutants) accumulate oxidized...
Tallennettuna:
| Päätekijät: | , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
National Academy of Sciences
1999
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC24128/ https://ncbi.nlm.nih.gov/pubmed/10570136 |
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