Robust folding of a de novo designed ideal protein even with most of the core mutated to valine

Protein design provides a stringent test for our understanding of protein folding. We previously described principles for designing ideal protein structures stabilized by consistent local and nonlocal interactions, based on a set of rules relating local backbone structures to tertiary packing motifs...

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Detalles Bibliográficos
Autores principales: Koga, Rie, Yamamoto, Mami, Kosugi, Takahiro, Kobayashi, Naohiro, Sugiki, Toshihiko, Fujiwara, Toshimichi, Koga, Nobuyasu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2020
Materias:
Biological Sciences
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7739874/
https://www.ncbi.nlm.nih.gov/pubmed/33229587
http://dx.doi.org/10.1073/pnas.2002120117

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7739874/
https://www.ncbi.nlm.nih.gov/pubmed/33229587
http://dx.doi.org/10.1073/pnas.2002120117

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