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

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-stat...

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Bibliographic Details
Published in:PloS one 2014-11, Vol.9 (11), p.e112374-e112374
Main Authors: Yao, Xuejun, Dürr, Ulrich H N, Gattin, Zrinka, Laukat, Yvonne, Narayanan, Rhagavendran L, Brückner, Ann-Kathrin, Meisinger, Chris, Lange, Adam, Becker, Stefan, Zweckstetter, Markus
Format: Article
Language:English
Subjects:
Analysis
Biochemistry
Biology and Life Sciences
Deuterium
Deuterium Exchange Measurement
Experiments
Foreign exchange rates
Fungal Proteins - chemistry
Hydrogen
Hydrogen ion concentration
Lipids
Liposomes - chemistry
Magnetic resonance spectroscopy
Membrane proteins
Membrane Proteins - chemistry
Mitochondria
Mitochondrial Proteins - chemistry
Neurospora crassa - chemistry
NMR
NMR spectroscopy
Nuclear magnetic resonance
Nuclear magnetic resonance spectroscopy
Nuclear Magnetic Resonance, Biomolecular
Physical Sciences
Protein transport
Protein Unfolding
Proteins
Research and analysis methods
Spectroscopy
Structural analysis
Translocation
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0112374