Article
Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.
Scientific reports - 6 May 2016
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
Abstract excerpt
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 spectroscopy and molecular dynamics simulations to compare the native state dynamics of Beta-2 microglobulin (β2m), whose...
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