Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution.

@article{Duan1998PathwaysTA,
  title={Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution.},
  author={Yong Duan and Peter A. Kollman},
  journal={Science},
  year={1998},
  volume={282 5389},
  pages={
          740-4
        }
}
An implementation of classical molecular dynamics on parallel computers of increased efficiency has enabled a simulation of protein folding with explicit representation of water for 1 microsecond, about two orders of magnitude longer than the longest simulation of a protein in water reported to date. Starting with an unfolded state of villin headpiece subdomain, hydrophobic collapse and helix formation occur in an initial phase, followed by conformational readjustments. A marginally stable… 

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