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A measure of helical propensity for amino acids in membrane environments

Nature Structural Biology volume 1, pages 368–373 (1994)Cite this article

An Erratum to this article was published on 01 August 1994

Abstract

The frequent occurrence of β-sheet promoting residues such as Ile, Val, and Thr in the α-helical transmembrane segments of most integral membrane proteins suggests that the helical propensities of these residues are altered in the hydrophobic environment of the lipid bilayer. Systematic studies of peptides by circular dichroism models spectroscopy in various micellar/vesicular media allow the establishment of a ranking order of helical propensity for uncharged amino acids in the membrane environment. In contrast to their conformational preferences in water, the helical proclivity of amino acids in membranes is shown to be governed by their side chain hydrophobicity, and by the hydropathy of the local peptide segments in which the residues reside.

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Authors and Affiliations

  1. Division of Biochemistry Research, Research Institute, The Hospital For Sick Children, Toronto, M5G 1X8

    Shun-Cheng Li & Charles M. Deber

  2. Department of Biochemistry, University of Toronto, Toronto, M5S 1A8, Ontario, Canada

    Shun-Cheng Li & Charles M. Deber

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  1. Shun-Cheng Li
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Li, SC., Deber, C. A measure of helical propensity for amino acids in membrane environments. Nat Struct Mol Biol 1, 368–373 (1994). https://doi.org/10.1038/nsb0694-368

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