Custom selenoprotein production enabled by laboratory evolution of recoded bacterial strains

Incorporation of the rare amino acid selenocysteine to form diselenide bonds can improve stability and function of synthetic peptide therapeutics. However, application of this approach to recombinant proteins has been hampered by heterogeneous incorporation, low selenoprotein yields, and poor fitnes...

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Detalles Bibliográficos
Autores principales: Thyer, Ross, Shroff, Raghav, Klein, Dustin R., d’Oelsnitz, Simon, Cotham, Victoria C., Byrom, Michelle, Brodbelt, Jennifer S., Ellington, Andrew D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6035053/
https://www.ncbi.nlm.nih.gov/pubmed/29863724
http://dx.doi.org/10.1038/nbt.4154

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6035053/
https://www.ncbi.nlm.nih.gov/pubmed/29863724
http://dx.doi.org/10.1038/nbt.4154

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