A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR.

@article{Petkova2002ASM,
  title={A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR.},
  author={Aneta T Petkova and Yoshitaka Ishii and John J. Balbach and Oleg N Antzutkin and Richard Leapman and Frank Delaglio and Robert Tycko},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2002},
  volume={99 26},
  pages={16742-7}
}
We present a structural model for amyloid fibrils formed by the 40-residue beta-amyloid peptide associated with Alzheimer's disease (Abeta(1-40)), based on a set of experimental constraints from solid state NMR spectroscopy. The model additionally incorporates the cross-beta structural motif established by x-ray fiber diffraction and satisfies constraints… CONTINUE READING