Polar and nonpolar atomic environments in the protein core: implications for folding and binding.

@article{Koehl1994PolarAN,
  title={Polar and nonpolar atomic environments in the protein core: implications for folding and binding.},
  author={Patrice Koehl and Marc Delarue},
  journal={Proteins},
  year={1994},
  volume={20 3},
  pages={264-78}
}
Hydrophobic interactions are believed to play an important role in protein folding and stability. Semi-empirical attempts to estimate these interactions are usually based on a model of solvation, whose contribution to the stability of proteins is assumed to be proportional to the surface area buried upon folding. Here we propose an extension of this idea by defining an environment free energy that characterizes the environment of each atom of the protein, including solvent, polar or nonpolar… CONTINUE READING

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