The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35.

@article{Gsponer2003TheRO,
  title={The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35.},
  author={Joerg Gsponer and Urs Haberth{\"u}r and Amedeo Caflisch},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 9},
  pages={5154-9}
}
Understanding the early steps of aggregation at atomic detail might be crucial for the rational design of therapeutics preventing diseases associated with amyloid deposits. In this paper, aggregation of the heptapeptide GNNQQNY, from the N-terminal prion-determining domain of the yeast protein Sup35, was studied by 20 molecular dynamics runs for a total simulation time of 20 micros. The simulations generate in-register parallel packing of GNNQQNY beta-strands that is consistent with x-ray… CONTINUE READING

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