In silico studies of protein misfolding and aggregation

Feb 24, 2011, 11:15 AM
FB42 (AlbaNova Main Building)


AlbaNova Main Building


Anders Irbäck (Lund University)


The aggregation of misfolded proteins into oligomers and fibrils has been linked to a variety of disorders such as Alzheimer's and Parkinson's diseases. The conformational mechanisms involved in the aggregation process remain incompletely understood. Here I present results from a Monte Carlo study of monomers and dimers of the 42-residue Abeta42 protein, associated with Alzheimer's disease. A comparison of results obtained for wild type Abeta42 and three mutants hints at specific conformational properties that might play a key role in aggregation. I also present results from an on-going study of protofibril formation for a 6-residue fragment of protein tau, based on simulations with up to 500 chains.

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