Speaker
Anders Irbäck
(Lund University)
Description
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.
