Influence of Gold Nanoparticles on the Kinetics of Alpha-Synuclein Aggregation

respect to the less stable mesophile. When focusing on different timeand lengthscales specific behaviors arise. At an atomistic scale, it is found that in the hyperthermophile a more regular alternation of rigid and flexible regions stabilizes a key part of the protein where the unfolding of the mesophile begins. We furthermore find that the conformational landscape of the hyperthermophile is characterized by a higher number of substates, or otherwise an enhanced conformational flexibility that is suggested to broaden its stability curve and raise the melting temperature. We finally compare, for the two proteins, the unfolding paths upon increasing temperature, the kinetic barrier along the early steps of unfolding and the temperature dependency of the stability. [1] A.Wrba, A. Schweiger, V. Schultes, R. Jaenicke, P. Zavodszky, Biochemistry, 1990, 29, 7584-7592. [2] J. Fitter, J. Heberle, Biophys. J, 2000, 79, 1629-1636.