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

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.

SUBMITTER: Yao X

PROVIDER: S-EPMC4223039 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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

Yao Xuejun X Dürr Ulrich H N UH Gattin Zrinka Z Laukat Yvonne Y Narayanan Rhagavendran L RL Brückner Ann-Kathrin AK Meisinger Chris C Lange Adam A Becker Stefan S Zweckstetter Markus M

PloS one 20141106 11

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 po ...[more]

PMID: 25375235

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