Electron Paramagnetic Resonance Spectroscopy Measures the Distance between the External beta-Strands of Folded alpha-Synuclein in Amyloid Fibrils
2011 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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Electron Paramagnetic Resonance Spectroscopy Measures the Distance between the External beta-Strands of Folded alpha-Synuclein in Amyloid Fibrils
Karyagina, I.; Becker, S. ; Giller, K. ; Riedel, D. ; Jovin, T. M. ; Griesinger, C. & Bennati, M. (2011)
Biophysical Journal, 101(1) pp. L1-L3. DOI: https://doi.org/10.1016/j.bpj.2011.05.052
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Details
- Authors
- Karyagina, Irina; Becker, Stefan ; Giller, Karin ; Riedel, Dietmar ; Jovin, Thomas M. ; Griesinger, Christian ; Bennati, Marina
- Abstract
- The misfolding of alpha-synuclein (alpha S) to a cross-beta-sheet amyloid structure is associated with pathological conditions in Parkinson's and other neurodegenerative diseases. Using pulse electron paramagnetic resonance spectroscopy combined with a cross-labeling strategy involving four double mutants, we were able to determine the intramolecular distance between the extremal beta-strands. The distance of 4.5 +/- 0.5 nm is in good agreement with the dimensions of a protofilament reported by other low-resolution techniques, such as x-ray scattering and atomic force microscopy.
- Issue Date
- 2011
- Journal
- Biophysical Journal
- ISSN
- 0006-3495
