The fold of alpha-synuclein fibrils.

@article{Vilar2008TheFO,
  title={The fold of alpha-synuclein fibrils.},
  author={Marçal Vilar and Hui-Ting Chou and Thorsten L{\"u}hrs and Samir K Maji and Dominique Riek-Loher and Ren{\'e} Verel and Gerard Manning and Henning Stahlberg and Roland Riek},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2008},
  volume={105 25},
  pages={8637-42}
}
The aggregation of proteins into amyloid fibrils is associated with several neurodegenerative diseases. In Parkinson's disease it is believed that the aggregation of alpha-synuclein (alpha-syn) from monomers by intermediates into amyloid fibrils is the toxic disease-causative mechanism. Here, we studied the structure of alpha-syn in its amyloid state by using various biophysical approaches. Quenched hydrogen/deuterium exchange NMR spectroscopy identified five beta-strands within the fibril core… CONTINUE READING
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