S. PornsuwanK. GillerD. RiedelS. BeckerC. GriesingerM. BennatiMax Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute)Universitat GottingenMahidol University2018-10-192018-10-192013-09-23Angewandte Chemie - International Edition. Vol.52, No.39 (2013), 10290-1029415213773143378512-s2.0-84884883488https://repository.li.mahidol.ac.th/handle/20.500.14594/31466Distance 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.Mahidol UniversityChemical EngineeringChemistryArticleSCOPUS10.1002/anie.201304747