Probing the initial stage of aggregation of the Abeta(10-35)-protein: assessing the propensity for peptide dimerization.

@article{Tarus2005ProbingTI,
  title={Probing the initial stage of aggregation of the Abeta(10-35)-protein: assessing the propensity for peptide dimerization.},
  author={Bogdan Tarus and John E. Straub and D. Thirumalai},
  journal={Journal of molecular biology},
  year={2005},
  volume={345 5},
  pages={1141-56}
}
Characterization of the early stages of peptide aggregation is of fundamental importance in elucidating the mechanism of the formation of deposits associated with amyloid disease. The initial step in the pathway of aggregation of the Abeta-protein, whose monomeric NMR structure is known, was studied through the simulation of the structure and stability of the peptide dimer in aqueous solution. A protocol based on shape complementarity was used to generate an assortment of possible dimer… CONTINUE READING