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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Detalhes bibliográficos
Publicado no:Sci Rep
Main Authors: 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
Formato: Artigo
Idioma:Inglês
Publicado em: Nature Publishing Group 2016
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Article
Acesso em linha: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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