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

Biophys J. 2011 Jul 6;101(1):L1-3. doi: 10.1016/j.bpj.2011.05.052.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amyloid
  • Electron Spin Resonance Spectroscopy
  • Humans
  • Molecular Sequence Data
  • Mutant Proteins / chemistry
  • Protein Folding*
  • Protein Structure, Secondary
  • alpha-Synuclein / chemistry*
  • alpha-Synuclein / metabolism*

Substances

  • Amyloid
  • Mutant Proteins
  • alpha-Synuclein