Dipoles of the α-helix and β-sheet: their role in protein folding

@article{Hol1981DipolesOT,
  title={Dipoles of the α-helix and β-sheet: their role in protein folding},
  author={Wim G. J. Hol and Louis M. Halie and Christian Sander},
  journal={Nature},
  year={1981},
  volume={294},
  pages={532-536}
}
As a result of the regular arrangement of peptide dipoles in secondary structure segments and the low effective dielectric constant in Hydrophobic cores, the electrostatic energy of a protein is very sensitive to the relative orientation of the segments. We provide here evidence that the alignment of secondary structure dipoles is significant in determining the three-dimensional structure of globular proteins. 

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