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Interaction of alpha-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement

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Rasia,  R. M.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Bertoncini,  C. W.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Ceolin,  M.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Jovin,  T. M.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Fernandez,  C. O.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Binolfi, A., Rasia, R. M., Bertoncini, C. W., Ceolin, M., Zweckstetter, M., Griesinger, C., et al. (2006). Interaction of alpha-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement. Journal of the American Chemical Society, 128(30), 9893-9901. Retrieved from http://pubs.acs.org/cgi-bin/article.cgi/jacsat/2006/128/i30/html/ja0618649.html.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-E41D-9
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