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Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability
A wide range of human diseases is associated with mutations that, destabilizing proteins native state, promote their aggregation. However, the mechanisms leading from folded to aggregated states are still incompletely understood. To investigate these mechanisms, we used a combination of NMR spectros...
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出版年: | Sci Rep |
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主要な著者: | , , , , , , , , , , , , |
フォーマット: | Artigo |
言語: | Inglês |
出版事項: |
Nature Publishing Group
2016
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主題: | |
オンライン・アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4858664/ https://ncbi.nlm.nih.gov/pubmed/27150430 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/srep25559 |
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