title: Electron paramagnetic resonance spectroscopy measures the distance between the external β-strands of folded α-synuclein in amyloid fibrils.
abstract: The misfolding of α-synuclein (αS) to a cross-β-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 β-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.
authors: RG Electron Spin Resonance Spectroscopy, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors: Irina
authors: I
authors: Karyagina
authors: Stefan
authors: S
authors: Becker
authors: Karin
authors: K
authors: Giller
authors: Dietmar
authors: D
authors: Riedel
authors: Thomas M
authors: TM
authors: Jovin
authors: Christian
authors: C
authors: Griesinger
authors: Marina
authors: M
authors: Bennati
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D008969:Molecular Sequence Data; D050505:Mutant Proteins / Q000737:chemistry; D017510:Protein Folding; D017433:Protein Structure, Secondary; D051844:alpha-Synuclein / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D000682:Amyloid; D050505:Mutant Proteins; D051844:alpha-Synuclein