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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Vydáno v:Sci Rep
Hlavní autoři: 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
Médium: Artigo
Jazyk:Inglês
Vydáno: Nature Publishing Group 2016
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Article
On-line přístup: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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