טוען...
Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm.
The thiol/disulfide oxidoreductase DsbA is the strongest oxidant of the thioredoxin superfamily and is required for efficient disulfide bond formation in the periplasm of Escherichia coli. To determine the importance of the redox potential of the final oxidant in periplasmic protein folding, we have...
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| Main Authors: | , , , |
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| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
1999
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| נושאים: | |
| גישה מקוונת: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1171408/ https://ncbi.nlm.nih.gov/pubmed/10369668 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/18.12.3271 |
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