Dipoles of the alpha-helix and beta-sheet: their role in protein folding
Hol, W.G.; Halie, L.M.; Sander, C.
Nature 294(5841): 532-536
1981
ISSN/ISBN: 0028-0836 PMID: 7312043 Document Number: 173520
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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