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Electron paramagnetic resonance spectroscopy measures the distance between the external β-strands of folded α-synuclein in amyloid fibrils.

MPS-Authors
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Karyagina,  I.
Research Group of Electron Paramagnetic Resonance, MPI for biophysical chemistry, Max Planck Society;

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

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Riedel,  D.
Facility for Electron Microscopy, 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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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Bennati,  M.
Research Group of Electron Paramagnetic Resonance, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

1051582.pdf
(Publisher version), 265KB

Supplementary Material (public)
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Citation

Karyagina, I., Becker, S., Giller, K., Riedel, D., Jovin, T. M., Griesinger, C., et al. (2011). Electron paramagnetic resonance spectroscopy measures the distance between the external β-strands of folded α-synuclein in amyloid fibrils. Biophysical Journal, 101(1), L1-L3.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-0E4E-B
Abstract
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