Amyloid beta-protein: experiment and theory on the 21-30 fragment.

@article{Murray2009AmyloidBE,
  title={Amyloid beta-protein: experiment and theory on the 21-30 fragment.},
  author={Megan M Murray and Mary Griffin Krone and Summer L. Bernstein and Andrij Baumketner and Margaret A M Condron and Noel D Lazo and David B Teplow and Thomas Wyttenbach and Joan-Emma Shea and Michael T. Bowers},
  journal={The journal of physical chemistry. B},
  year={2009},
  volume={113 17},
  pages={6041-6}
}
The structure of the 21-30 fragment of the amyloid beta-protein (Abeta) was investigated by ion mobility mass spectrometry and replica exchange dynamics simulations. Mutations associated with familial Alzheimer's disease (E22G, E22Q, E22K, and D23N) of Abeta(21-30) were also studied, in order to understand any structural changes that might occur with these substitutions. The structure of the WT peptide shows a bend and a perpendicular turn in the backbone which is maintained by a network of D23… CONTINUE READING

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