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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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書誌詳細
出版年:Sci Rep
主要な著者: Camilloni, Carlo, Sala, Benedetta Maria, Sormanni, Pietro, Porcari, Riccardo, Corazza, Alessandra, De Rosa, Matteo, Zanini, Stefano, Barbiroli, Alberto, Esposito, Gennaro, Bolognesi, Martino, Bellotti, Vittorio, Vendruscolo, Michele, Ricagno, Stefano
フォーマット: Artigo
言語:Inglês
出版事項: Nature Publishing Group 2016
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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