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Putting the β-breaks on membrane protein misfolding

Nature Structural Biology volume 9, pages 318–319 (2002)Cite this article

Proline in transmembrane helical segments is thought to play specific roles in membrane protein structure and function. Yet one of its primary contributions may occur even before the segment enters the membrane.

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Figure 1: Properties of a proline residue in the context of an α-helix.
Figure 2: Possible roles of proline in transmembrane helical segments of membrane proteins.

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Acknowledgements

C.M.D. is supported by grants from the Canadian Institutes of Health Research (CIHR) and the Canadian Cystic Fibrosis Foundation (CCFF). A.G.T. holds a CIHR postdoctoral fellowship.

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Authors and Affiliations

  1. Division of Structural Biology and Biochemistry, Research Institute, Hospital for Sick Children, 555 University Avenue, Room 3427A, Toronto, M5G 1X8, Ontario, Canada

    Charles M. Deber & Alex G. Therien

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

    Charles M. Deber & Alex G. Therien

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  1. Charles M. Deber
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Correspondence to Charles M. Deber.

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Deber, C., Therien, A. Putting the β-breaks on membrane protein misfolding. Nat Struct Mol Biol 9, 318–319 (2002). https://doi.org/10.1038/nsb0502-318

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