Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix.

@article{Blake1996SynchrotronXS,
  title={Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix.},
  author={Colin C. F. Blake and Louise C. Serpell},
  journal={Structure},
  year={1996},
  volume={4 8},
  pages={989-98}
}
BACKGROUND Amyloid diseases, which include Alzheimer's disease and the transmissible spongiform encephalopathies, are characterized by the extracellular deposition of abnormal protein fibrils derived from soluble precursor proteins. Although different precursors seem to generate similar fibrils, no adequate molecular structure of amyloid fibrils has been produced using modern techniques. Knowledge of the fibril structure is essential to understanding the molecular mechanism of amyloid formation… CONTINUE READING
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