Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy
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 pos...
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th-mahidol.314662018-10-19T11:47:09Z Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy S. Pornsuwan K. Giller D. Riedel S. Becker C. Griesinger M. Bennati Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute) Universitat Gottingen Mahidol University Chemical Engineering Chemistry 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. © 2013 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution Non-Commercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. 2018-10-19T04:45:10Z 2018-10-19T04:45:10Z 2013-09-23 Article Angewandte Chemie - International Edition. Vol.52, No.39 (2013), 10290-10294 10.1002/anie.201304747 15213773 14337851 2-s2.0-84884883488 https://repository.li.mahidol.ac.th/handle/123456789/31466 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84884883488&origin=inward |
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Chemical Engineering Chemistry S. Pornsuwan K. Giller D. Riedel S. Becker C. Griesinger M. Bennati Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy |
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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. © 2013 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution Non-Commercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
author2 |
Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute) |
author_facet |
Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute) S. Pornsuwan K. Giller D. Riedel S. Becker C. Griesinger M. Bennati |
format |
Article |
author |
S. Pornsuwan K. Giller D. Riedel S. Becker C. Griesinger M. Bennati |
author_sort |
S. Pornsuwan |
title |
Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy |
title_short |
Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy |
title_full |
Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy |
title_fullStr |
Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy |
title_full_unstemmed |
Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy |
title_sort |
long-range distances in amyloid fibrils of α-synuclein from peldor spectroscopy |
publishDate |
2018 |
url |
https://repository.li.mahidol.ac.th/handle/123456789/31466 |
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1763488223303041024 |