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The α-helix dipole and the properties of proteins

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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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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