Dissecting the stability determinants of a challenging de novo protein fold using massively parallel design and experimentation

Designing entirely new protein structures remains challenging because we do not fully understand the biophysical determinants of folding stability. Yet, some protein folds are easier to design than others. Previous work identified the 43-residue ɑββɑ fold as especially challenging: The best designs...

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Detalles Bibliográficos
Autores principales: Kim, Tae-Eun, Tsuboyama, Kotaro, Houliston, Scott, Martell, Cydney M., Phoumyvong, Claire M., Lemak, Alexander, Haddox, Hugh K., Arrowsmith, Cheryl H., Rocklin, Gabriel J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2022
Materias:
Biological Sciences
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9564214/
https://www.ncbi.nlm.nih.gov/pubmed/36191185
http://dx.doi.org/10.1073/pnas.2122676119

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9564214/
https://www.ncbi.nlm.nih.gov/pubmed/36191185
http://dx.doi.org/10.1073/pnas.2122676119

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