Absolute comparison of simulated and experimental protein-folding dynamics

  title={Absolute comparison of simulated and experimental protein-folding dynamics},
  author={Christopher D. Snow and Houbi Nguyen and Vijay S. Pande and Martin Gruebele},
Protein folding is difficult to simulate with classical molecular dynamics. Secondary structure motifs such as α-helices and β-hairpins can form in 0.1–10 µs (ref. 1), whereas small proteins have been shown to fold completely in tens of microseconds. The longest folding simulation to date is a single 1-µs simulation of the villin headpiece; however, such single runs may miss many features of the folding process as it is a heterogeneous reaction involving an ensemble of transition states. Here… 
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