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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Detalles Bibliográficos
Autores principales: 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: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4858664/
https://www.ncbi.nlm.nih.gov/pubmed/27150430
http://dx.doi.org/10.1038/srep25559

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4858664/
https://www.ncbi.nlm.nih.gov/pubmed/27150430
http://dx.doi.org/10.1038/srep25559

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