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    Spontaneous transmembrane helix insertion thermodynamically mimics translocon-guided insertion

    Ulmschneider, M.B. and Ulmschneider, J.P. and Schiller, N. and Wallace, Bonnie A. and von Heijne, G. and White, S.H. (2014) Spontaneous transmembrane helix insertion thermodynamically mimics translocon-guided insertion. Nature Communications 5 , p. 4863. ISSN 2041-1723.

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    Abstract

    The favourable transfer free energy for a transmembrane (TM) α-helix between the aqueous phase and lipid bilayer underlies the stability of membrane proteins. However, the connection between the energetics and process of membrane protein assembly by the Sec61/​SecY translocon complex in vivo is not clear. Here, we directly determine the partitioning free energies of a family of designed peptides using three independent approaches: an experimental microsomal Sec61 translocon assay, a biophysical (spectroscopic) characterization of peptide insertion into hydrated planar lipid bilayer arrays, and an unbiased atomic-detail equilibrium folding-partitioning molecular dynamics simulation. Remarkably, the measured free energies of insertion are quantitatively similar for all three approaches. The molecular dynamics simulations show that TM helix insertion involves equilibrium with the membrane interface, suggesting that the interface may play a role in translocon-guided insertion.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): Biological sciences, Cell biology
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Bioinformatics, Bloomsbury Centre for, Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 15 Sep 2014 09:15
    Last Modified: 07 Dec 2016 15:05
    URI: http://eprints.bbk.ac.uk/id/eprint/10518

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