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- W2059640916 abstract "Amide hydrogen/deuterium exchange (HDX) rate constants of bovine ubiquitin in an ammonium acetate solution containing 1% of the electrospray ionization (ESI) supercharging reagent m-nitrobenzyl alcohol (m-NBA) were obtained using top-down, electron transfer dissociation (ETD) tandem mass spectrometry (MS). The supercharging reagent replaces the acid and temperature quench step in the conventional MS approach to HDX experiments by causing rapid protein denaturation to occur in the ESI droplet. The higher charge state ions that are produced with m-NBA are more unfolded, as measured by ion mobility, and result in higher fragmentation efficiency and higher sequence coverage with ETD. Single amino acid resolution was obtained for 44 of 72 exchangeable amide sites, and summed kinetic data were obtained for regions of the protein where adjacent fragment ions were not observed, resulting in an overall spatial resolution of 1.3 residues. Comparison of these results with previous values from NMR indicates that the supercharging reagent does not cause significant structural changes to the protein in the initial ESI solution and that scrambling or back-exchange is minimal. This new method for top-down HDX-MS enables real-time kinetic data measurements under physiological conditions, similar to those obtained using NMR, with comparable spatial resolution and significantly better sensitivity." @default.
- W2059640916 created "2016-06-24" @default.
- W2059640916 creator A5014296444 @default.
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- W2059640916 date "2010-10-13" @default.
- W2059640916 modified "2023-10-18" @default.
- W2059640916 title "Real-Time Hydrogen/Deuterium Exchange Kinetics via Supercharged Electrospray Ionization Tandem Mass Spectrometry" @default.
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- W2059640916 doi "https://doi.org/10.1021/ac101957x" @default.
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