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Journal Article

Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy.

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

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Giller,  K.
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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Becker,  S.
Department of NMR Based Structural 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;

External Resource

http://onlinelibrary.wiley.com/doi/10.1002/anie.201304747/pdf
(Publisher version)

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Fulltext (public)

1835489.pdf
(Publisher version), 945KB

Supplementary Material (public)

1835489_Supplement_1.pdf
(Supplementary material), 3MB

Citation

Pornsuwan, S., Giller, K., Riedel, D., Becker, S., Griesinger, C., & Bennati, M. (2013). Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy. Angewandte Chemie International Edition, 52(39), 10290-10294. doi:10.1002/anie.201304747.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0014-4DFD-F
Abstract
Distance measurements: Pulsed EPR distance measurements combined with strategic spin labeling provide structural constraints at the molecular level for the fold of α-synuclein in amyloid fibrils (see picture; r=distance). The detection of interstrand distances in fibrils will potentially make it possible to extend these measurements to oligomeric states of these protein families.