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

Nature volume 294, pages 532–536 (1981)Cite this article

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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Authors and Affiliations

  1. Laboratory of Chemical Physics, Department of Chemistry, University of Groningen, Nijenborgh 16, 9747 AG, Groningen, The Netherlands

    Wim G. J. Hol & Louis M. Halie

  2. Biophysics Department, Max Planck Institute of Medical Research, Jahnstrasse 29, Heidelberg, FRG

    Christian Sander

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  1. Wim G. J. Hol
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  2. Louis M. Halie
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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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