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The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35

Understanding the early steps of aggregation at atomic detail might be crucial for the rational design of therapeutics preventing diseases associated with amyloid deposits. In this paper, aggregation of the heptapeptide GNNQQNY, from the N-terminal prion-determining domain of the yeast protein Sup35...

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Библиографические подробности
Опубликовано в::Proc Natl Acad Sci U S A
Главные авторы: Gsponer, Jörg, Haberthür, Urs, Caflisch, Amedeo
Формат: Artigo
Язык:Inglês
Опубликовано: National Academy of Sciences 2003
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Online-ссылка:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC154314/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12700355/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.0835307100
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