Kinetics of amyloid beta monomer-to-oligomer exchange by NMR relaxation.

@article{Fawzi2010KineticsOA,
  title={Kinetics of amyloid beta monomer-to-oligomer exchange by NMR relaxation.},
  author={Nicolas L. Fawzi and Jinfa Ying and Dennis A. Torchia and G Marius Clore},
  journal={Journal of the American Chemical Society},
  year={2010},
  volume={132 29},
  pages={9948-51}
}
Recent studies have implicated non-fibrillar oligomers of the amyloid beta (Abeta) peptide as the primary toxic species in Alzheimer's disease. Detailed structural and kinetic characterization of these states, however, has been difficult. Here we use NMR relaxation measurements to address the kinetics of exchange between monomeric and large, polymorphic oligomeric species of Abeta(1-40). (15)N and (1)H(N) R(2) data at multiple magnetic fields were recorded for several peptide concentrations… CONTINUE READING
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