C-terminal turn stability determines assembly differences between Aβ40 and Aβ42.

@article{Roychaudhuri2013CterminalTS,
  title={C-terminal turn stability determines assembly differences between Aβ40 and Aβ42.},
  author={Robin Roychaudhuri and Mingfeng Yang and Atul Deshpande and Gregory M. Cole and Sally Ann Frautschy and Aleksey Lomakin and George B. Benedek and David B Teplow},
  journal={Journal of molecular biology},
  year={2013},
  volume={425 2},
  pages={292-308}
}
Oligomerization of the amyloid β-protein (Aβ) is a seminal event in Alzheimer's disease. Aβ42, which is only two amino acids longer than Aβ40, is particularly pathogenic. Why this is so has not been elucidated fully. We report here results of computational and experimental studies revealing a C-terminal turn at Val36-Gly37 in Aβ42 that is not present in Aβ40. The dihedral angles of residues 36 and 37 in an Ile31-Ala42 peptide were consistent with β-turns, and a β-hairpin-like structure was… CONTINUE READING