Modification and optimization of the united-residue (UNRES) potential energy function for canonical simulations. I. Temperature dependence of the effective energy function and tests of the optimization method with single training proteins.

@article{Liwo2007ModificationAO,
  title={Modification and optimization of the united-residue (UNRES) potential energy function for canonical simulations. I. Temperature dependence of the effective energy function and tests of the optimization method with single training proteins.},
  author={Adam Liwo and Mey Khalili and Cezary Czaplewski and Sebastian Kalinowski and Staniłsaw Ołdziej and Katarzyna Wachucik and Harold A. Scheraga},
  journal={The journal of physical chemistry. B},
  year={2007},
  volume={111 1},
  pages={260-85}
}
We report the modification and parametrization of the united-residue (UNRES) force field for energy-based protein structure prediction and protein folding simulations. We tested the approach on three training proteins separately: 1E0L (beta), 1GAB (alpha), and 1E0G (alpha + beta). Heretofore, the UNRES force field had been designed and parametrized to locate native-like structures of proteins as global minima of their effective potential energy surfaces, which largely neglected the… CONTINUE READING

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