SAS: Split antibiotic selection for identifying chaperones that improve protein solubility.

ABSTRACT:

Background

Heterologous expression of active, native-folded protein in Escherichia coli is critical in both academic research and biotechnology settings. When expressing non-native recombinant proteins in E. coli, obtaining soluble and active protein can be challenging. Numerous techniques can be used to enhance a proteins solubility, and largely focus on either altering the expression strain, plasmid vector features, growth conditions, or the protein coding sequence itself. However, there is no one-size-fits-all approach for addressing issues with protein solubility, and it can be both time and labor intensive to find a solution. An alternative approach is to use the co-expression of chaperones to assist with increasing protein solubility. By designing a genetic syst

SUBMITTER: McNutt E 

PROVIDER: S-EPMC10943334 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature