Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability

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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Bibliographic Details
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
Format: Online
Language:English
Published: Nature Publishing Group 2016
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4858664/

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https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4858664/

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