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The α-helix dipole and the properties of proteins

Nature volume 273, pages 443–446 (1978)Cite this article

Abstract

Phosphate moieties bind frequently at N-termini of helices in proteins. It is shown that this corresponds with an optimal interaction of the helix dipole and the charged phosphate. This favourable arrangement may have been discovered several times during evolution. In some enzymes, the helix dipole might be used in catalysis.

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Authors and Affiliations

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

    W. G. J. Hol, P. T. van Duijnen & H. J. C. Berendsen

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  1. W. G. J. Hol
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  2. P. T. van Duijnen
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  3. H. J. C. Berendsen
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Hol, W., van Duijnen, P. & Berendsen, H. The α-helix dipole and the properties of proteins. Nature 273, 443–446 (1978). https://doi.org/10.1038/273443a0

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