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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-4DFD-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CD96-C
Genre: Journal Article

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 Creators:
Pornsuwan, S.1, Author              
Giller, K.2, Author              
Riedel, D.3, Author              
Becker, S.2, Author              
Griesinger, C.2, Author              
Bennati, M.1, Author              
Affiliations:
1Research Group of Electron Paramagnetic Resonance, MPI for biophysical chemistry, Max Planck Society, ou_578606              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
3Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              

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 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.

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Language(s): eng - English
 Dates: 2013-08-092013-09-23
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201304747
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 52 (39) Sequence Number: - Start / End Page: 10290 - 10294 Identifier: -