NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins.
basic_science · Level V
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- Record sourced from PubMed, PMID 25375235.
- Also identified by DOI 10.1371/journal.pone.0112374 and PMC identifier PMC3012482.
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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.