Abstract
A number of diseases, known as amyloid diseases, are associated with pathological protein folding. Incorrectly or partially folded peptides or proteins can self-assemble into a variety of neurotoxic aggregate species, ranging from small soluble oligomers to amyloid fibrils. I will introduce a novel off-lattice coarse-grained peptide model that can be used to simulate the aggregation process from monomers to fibrils. The effects of beta-sheet propensity and of surfaces on the morphology of the aggregates will be discussed.
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