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Protein solubility and differential proteomic profiling of recombinant Escherichia coli overexpressing double-tagged fusion proteins
Chung-Hsien Cheng, Wen-Chien Lee
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50% confidenceThis study investigates the solubility and proteomic profiling of recombinant E. coli overexpressing double-tagged fusion proteins, with potential implications for microbial electrolysis cell applications.
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Abstract
Key findings
- The study found that the solubility of the fusion proteins was significantly improved compared to the wild-type protein.
- Differential proteomic profiling revealed changes in protein expression and modification in response to the overexpression of the double-tagged fusion proteins.
- The results suggest that the double-tagged fusion proteins may have improved stability and functionality, which could be beneficial for microbial electrolysis cell applications.
Keywords
BiochemistryAldolase AEscherichia coliFusion proteinProteomeRecombinant DNA
Identifiers
- Journal
- Microbial Cell Factories
- Year
- 2009