Computer simulation of protein folding

@article{Levitt1975ComputerSO,
  title={Computer simulation of protein folding},
  author={Michael Levitt and Arieh Warshel},
  journal={Nature},
  year={1975},
  volume={253},
  pages={694-698}
}
A new and very simple representation of protein conformations has been used together with energy minimisation and thermalisation to simulate protein folding. Under certain conditions, the method succeeds in ‘renaturing’ bovine pancreatic trypsin inhibitor from an open-chain conformation into a folded conformation close to that of the native molecule. 
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Many characteristics expected of true proteins, such as the sequence‐dependent formation of secondary structure, the partitioning of hydrophobic residues, and specific disulfide, are suggested so that the model may accurately simulate the folding process.
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