Abstract
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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Hol, W., Halie, L. & Sander, C. Dipoles of the α-helix and β-sheet: their role in protein folding. Nature 294, 532–536 (1981). https://doi.org/10.1038/294532a0
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DOI: https://doi.org/10.1038/294532a0
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