Cargando…
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...
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: | |
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 |
Ejemplares similares
-
Real-time observation of functional specialization among phosphorylation sites in CFTR
por: Infield, Daniel T., et al.
Publicado: (2023) -
Orthogonality of Pyrrolysine tRNA in the Xenopus oocyte
por: Infield, Daniel T., et al.
Publicado: (2018) -
Replacing voltage sensor arginines with citrulline provides mechanistic insight into charge versus shape
por: Infield, Daniel T., et al.
Publicado: (2018) -
Main-chain mutagenesis reveals intrahelical coupling in an ion channel voltage-sensor
por: Infield, Daniel T., et al.
Publicado: (2018) -
Fluorinated phenylalanines: synthesis and pharmaceutical applications
por: Awad, Laila Fathy, et al.
Publicado: (2020)