NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins
06.11.2014
Yao X, Dürr UH, Gattin Z, Laukat Y, Narayanan RL, Brückner AK, Meisinger C, Lange A, Becker S, Zweckstetter M.
PLoS One. 2014;9(11):e112374
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.
