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Intermediates in the folding of the membrane protein bacteriorhodopsin

Nature Structural Biology volume 2, pages 139–143 (1995)Cite this article

Abstract

Assembly of proteins within lipid bilayers is essential for the biogenesis and function of biological membranes. Little is known, however, about the underlying mechanism of assembly, and it is not clear whether it is possible to observe individual folding steps for integral membrane proteins either in vivo or in vitro. Fluorescence spectroscopy is used here to follow the time course of folding events for bacteriorhodopsin in mixed detergent/Iipid micelles. Transient folding-intermediates are detected and binding of the retinal chromophore occurs at a late stage, when it binds to an apoprotein intermediate.

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Author notes

  1. Lawrence J. Stern

    Present address: Department of Biochemistry and Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts, USA

Authors and Affiliations

  1. Department of Biochemistry, University of Oxford, South Parks Road, Oxford, UK

    Paula J. Booth

  2. Dyson Perrins Laboratory, University of Oxford, South Parks Road, Oxford, UK

    Sabine L. Flitsch

  3. Department of Biology and Chemistry, Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA

    Lawrence J. Stern, Duncan A. Greenhalgh & H. Gobind Khorana

  4. Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA

    Peter S. Kim

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  2. Sabine L. Flitsch
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  4. Duncan A. Greenhalgh
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  5. Peter S. Kim
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  6. H. Gobind Khorana
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Booth, P., Flitsch, S., Stern, L. et al. Intermediates in the folding of the membrane protein bacteriorhodopsin. Nat Struct Mol Biol 2, 139–143 (1995). https://doi.org/10.1038/nsb0295-139

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