Abeta42 is more rigid than Abeta40 at the C terminus: implications for Abeta aggregation and toxicity.

@article{Yan2006Abeta42IM,
  title={Abeta42 is more rigid than Abeta40 at the C terminus: implications for Abeta aggregation and toxicity.},
  author={Yilin Yan and Chunyu Wang},
  journal={Journal of molecular biology},
  year={2006},
  volume={364 5},
  pages={853-62}
}
Abeta40 and Abeta42 are the major forms of amyloid beta peptides (Abeta) in the brain. Although Abeta42 differs from Abeta40 by only two residues, Abeta42 is much more prone to aggregation and more toxic to neurons than Abeta40. To probe whether dynamics contribute to such dramatic difference in function, backbone ps-ns dynamics of native Abeta monomers were characterized by 15N spin relaxation at 273.3 K and 800 MHz. Abeta42 aggregates much faster than Abeta40 in the NMR tube. The effect of… CONTINUE READING