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Spontaneous transmembrane helix insertion thermodynamically mimics translocon-guided insertion

Author

Listed:
  • Martin B. Ulmschneider

    (Johns Hopkins University)

  • Jakob P. Ulmschneider

    (Shanghai Jiao Tong University)

  • Nina Schiller

    (Center for Biomembrane Research, Stockholm University
    Science for Life Laboratory, Stockholm University)

  • B. A. Wallace

    (Institute of Structural and Molecular Biology, Birkbeck College, University of London)

  • Gunnar von Heijne

    (Center for Biomembrane Research, Stockholm University
    Science for Life Laboratory, Stockholm University)

  • Stephen H. White

    (University of California)

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.

Suggested Citation

  • Martin B. Ulmschneider & Jakob P. Ulmschneider & Nina Schiller & B. A. Wallace & Gunnar von Heijne & Stephen H. White, 2014. "Spontaneous transmembrane helix insertion thermodynamically mimics translocon-guided insertion," Nature Communications, Nature, vol. 5(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5863
    DOI: 10.1038/ncomms5863
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    Cited by:

    1. Jakob P. Ulmschneider & Martin B. Ulmschneider, 2024. "Melittin can permeabilize membranes via large transient pores," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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