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

Hol, Wim G. J.; Halie, Louis M.; Sander, Christian

doi:10.1038/294532a0

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

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Sander, Christian
Max Planck Institute for Medical Research, Max Planck Society;

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Hol, W. G. J., Halie, L. M., & Sander, C. (1981). Dipoles of the α-helix and β-sheet: their role in protein folding. Nature, 294(5841), 532-536. doi:10.1038/294532a0.

Cite as: https://hdl.handle.net/21.11116/0000-0004-E676-4

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.