articleProceedings of the National Academy of SciencesOct 24, 2005GREEN OA

Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR

HHHenrike HeiseWHWolfgang HoyerSBStefan BeckerOCOvidiu C. AndronesiDRDietmar Riedel

Max Planck Institute for Biophysical Chemistry

PubMed
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Abstract

The 140-residue protein alpha-synuclein (AS) is able to form amyloid fibrils and as such is the main component of protein inclusions involved in Parkinson's disease. We have investigated the structure and dynamics of full-length AS fibrils by high-resolution solid-state NMR spectroscopy. Homonuclear and heteronuclear 2D and 3D spectra of fibrils grown from uniformly (13)C/(15)N-labeled AS and AS reverse-labeled for two of the most abundant amino acids, K and V, were analyzed. (13)C and (15)N signals exhibited linewidths of

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Topics & keywords

Topics
Keywords
  • Fibril
  • Chemistry
  • Crystallography
  • Solid-state nuclear magnetic resonance
  • Heteronuclear molecule
  • Protein secondary structure
  • Chemical shift
  • Monomer
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