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Structural and functional diversity in 4-α-helical proteins

Nature volume 287, pages 82–84 (1980)Cite this article

Abstract

Protein crystallographic studies show that many structural arrangements appear as common features among proteins which are otherwise unrelated in sequence or function. One of the more recently recognized recurring protein structural motifs is a nearly parallel arrangement of four α-helices to form a sequentially connected left-twisted bundle1. We describe here the geometrical properties of these structures and suggest how they relate to the functional and aggregate properties of these molecules.

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Authors and Affiliations

  1. Department of Biochemistry, New Chemistry Building, University of Arizona, Tucson, Arizona, 85721

    Patricia C. Weber & F. R. Salemme

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  1. Patricia C. Weber
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  2. F. R. Salemme
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Weber, P., Salemme, F. Structural and functional diversity in 4-α-helical proteins. Nature 287, 82–84 (1980). https://doi.org/10.1038/287082a0

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