Efficient rotamer elimination applied to protein side-chains and related spin glasses.

@article{Goldstein1994EfficientRE,
  title={Efficient rotamer elimination applied to protein side-chains and related spin glasses.},
  author={Robert F. Goldstein},
  journal={Biophysical journal},
  year={1994},
  volume={66 5},
  pages={
          1335-40
        }
}
Folded proteins and spin glasses share various properties, such as seemingly random interactions between residues (spins), and one might presume that some generic behaviors of spin glasses would also be exhibited in a general way by proteins. But a comparison here shows that the side-chain conformation systems of apo-myoglobin and lysozyme are qualitatively different from specific closely related spin glass systems. This difference is manifest in the number of rotamers that can be identified as… CONTINUE READING
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