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Electron paramagnetic resonance spectroscopy measures the distance between the external ?-strands of folded ?-synuclein in amyloid fibrils.

ABSTRACT: The misfolding of ?-synuclein (?S) to a cross-?-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 ?-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.

SUBMITTER: Karyagina I

PROVIDER: S-EPMC3127190 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Electron paramagnetic resonance spectroscopy measures the distance between the external β-strands of folded α-synuclein in amyloid fibrils.

Karyagina Irina I Becker Stefan S Giller Karin K Riedel Dietmar D Jovin Thomas M TM Griesinger Christian C Bennati Marina M

Biophysical journal 20110701 1

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-resolut ...[more]

PMID: 21723808

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