First Passage Analysis of the Folding of a β-Sheet Miniprotein: Is it More Realistic Than the Standard Equilibrium Approach?

@inproceedings{Kalgin2014FirstPA,
  title={First Passage Analysis of the Folding of a β-Sheet
Miniprotein: Is it More Realistic Than the Standard Equilibrium Approach?},
  author={Igor V. Kalgin and Sergei F Chekmarev and Martin Karplus},
  booktitle={The journal of physical chemistry. B},
  year={2014}
}
Simulations of first-passage folding of the antiparallel β-sheet miniprotein beta3s, which has been intensively studied under equilibrium conditions by A. Caflisch and co-workers, show that the kinetics and dynamics are significantly different from those for equilibrium folding. Because the folding of a protein in a living system generally corresponds to the former (i.e., the folded protein is stable and unfolding is a rare event), the difference is of interest. In contrast to equilibrium… CONTINUE READING
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