The microtubule associated protein tau is essential for the development and maintenance of the nervous system.  Tau dysfunction is associated with a class of diseases called tauopathies, in which tau is found in an aggregated form. I will present atomistic simulations of the initial stages of aggregation of this peptide, and discuss the effect of point mutations, pH, and osmolytes on the folding and assembly of this intrinsically disordered peptide. These studies will be complemented by simulations that employ an off-lattice, coarse-grained description of the peptide. The latter overcome some of the computational obstacles that plague atomistic simulations, and can be used to simulate the entire aggregation process from monomers to fibrils.

Atomistic and coarse-grained simulations of the self-assembly of the tau peptide

247th National Meeting (2014)

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