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Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein

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Kim,  H. Y.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Heise,  H.
Research Group of Solid State NMR Spectroscopy, 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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Baldus,  M.
Research Group of Solid State NMR Spectroscopy, 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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Kim, H. Y., Heise, H., Fernandez, C. O., Baldus, M., & Zweckstetter, M. (2007). Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein. ChemBioChem, 8(14), 1671-1674. Retrieved from http://www3.interscience.wiley.com/cgi-bin/fulltext/115806778/HTMLSTART.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-E2C2-1
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