Tuning phenylalanine fluorination to assess aromatic contributions to protein function and stability in cells

The aromatic side-chains of phenylalanine, tyrosine, and tryptophan interact with their environments via both hydrophobic and electrostatic interactions. Determining the extent to which these contribute to protein function and stability is not possible with conventional mutagenesis. Serial fluorinat...

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Detalles Bibliográficos
Autores principales: Galles, Grace D., Infield, Daniel T., Clark, Colin J., Hemshorn, Marcus L., Manikandan, Shivani, Fazan, Frederico, Rasouli, Ali, Tajkhorshid, Emad, Galpin, Jason D., Cooley, Richard B., Mehl, Ryan A., Ahern, Christopher A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9813137/
https://www.ncbi.nlm.nih.gov/pubmed/36599844
http://dx.doi.org/10.1038/s41467-022-35761-w

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9813137/
https://www.ncbi.nlm.nih.gov/pubmed/36599844
http://dx.doi.org/10.1038/s41467-022-35761-w

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