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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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Pubblicato in:Proc Natl Acad Sci U S A
Autori principali: Koga, Rie, Yamamoto, Mami, Kosugi, Takahiro, Kobayashi, Naohiro, Sugiki, Toshihiko, Fujiwara, Toshimichi, Koga, Nobuyasu
Natura: Artigo
Lingua:Inglês
Pubblicazione: National Academy of Sciences 2020
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC7739874/
https://ncbi.nlm.nih.gov/pubmed/33229587
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.2002120117
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