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

Nature volume 294, pages 532536 (10 December 1981) | Download Citation

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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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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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https://doi.org/10.1038/294532a0

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