Automated design of the surface positions of protein helices.

@article{Dahiyat1997AutomatedDO,
  title={Automated design of the surface positions of protein helices.},
  author={Bassil I Dahiyat and D. Benjamin Gordon and Stephen L. Mayo},
  journal={Protein science : a publication of the Protein Society},
  year={1997},
  volume={6 6},
  pages={1333-7}
}
Using a protein design algorithm that quantitatively considers side-chain interactions, the design of surface residues of alpha helices was examined. Three scoring functions were tested: a hydrogen-bond potential, a hydrogen-bond potential in conjunction with a penalty for uncompensated burial of polar hydrogens, and a hydrogen-bond potential in combination with helix propensity. The solvent exposed residues of a homodimeric coiled coil based on GCN4-p1 were designed by using the Dead-End… CONTINUE READING
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