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Journal Article

NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins.

MPS-Authors
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Yao,  X.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Dürr,  U. H. N.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Gattin,  Z.
Research Group of Solid-state NMR, MPI for biophysical chemistry, Max Planck Society;

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Laukat,  Y.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Narayanan,  R.L.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

Fulltext (public)

2072875.pdf
(Publisher version), 2MB

Supplementary Material (public)

2072875_Suppl_1.tif
(Supplementary material), 479KB

2072875_Suppl_2.tif
(Supplementary material), 557KB

2072875_Suppl_3.tif
(Supplementary material), 625KB

2072875_Suppl_4.doc
(Supplementary material), 40KB

Citation

Yao, X., Dürr, U. H. N., Gattin, Z., Laukat, Y., Narayanan, R., Brückner, A. K., et al. (2014). NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins. PLOS One, 9(11): e112374. doi:10.1371/journal.pone.0112374.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-4000-3
Abstract
Membrane proteins play key roles in biology. Determination of their structure in a membrane environment, however, is highly challenging. To address this challenge, we developed an approach that couples hydrogen/deuterium exchange of membrane proteins to rapid unfolding and detection by solution-state NMR spectroscopy. We show that the method allows analysis of the solvent protection of single residues in liposome-embedded proteins such as the 349-residue Tom40, the major protein translocation pore in the outer mitochondrial membrane, which has resisted structural analysis for many years.