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- W2022359852 abstract "A method for measuring site-specific amide hydrogen-deuterium exchange rates for membrane proteins in bilayers is reported and evaluated. This method represents an adaptation and extension of the approach of Dempsey and co-workers (Biophys. J. 70, 1777-1788 (1996)) and is based on reconstituting (15)N-labeled membrane proteins into phospholipid bilayers, followed by lyophilization and rehydration with D(2)O or H(2)O (control). Following incubation for a time t under hydrated conditions, samples are again lyophilized and then solubilized in an organic solvent system, where (1)H-(15)N HSQC spectra are recorded. Comparison of spectra from D(2)O-exposed samples to spectra from control samples yields the extent of the H-D exchange which occurred in the bilayers during time t. Measurements are site specific if specific (15)N labeling is used. The first part of this paper deals with the search for a suitable solvent system in which to solubilize complex membrane proteins in an amide exchange-trapped form for NMR quantitation of amide peak intensities. The second portion of the paper documents application of the overall procedure to measuring site-specific amide exchange rates in diacylglycerol kinase, a representative integral membrane protein. Both the potential usefulness and the significant limitations of the new method are documented." @default.
- W2022359852 created "2016-06-24" @default.
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- W2022359852 date "2000-01-01" @default.
- W2022359852 modified "2023-10-15" @default.
- W2022359852 title "NMR-Based Amide Hydrogen–Deuterium Exchange Measurements for Complex Membrane Proteins: Development and Critical Evaluation" @default.
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- W2022359852 doi "https://doi.org/10.1006/jmre.1999.1920" @default.
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