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Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
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April 17, 2017
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Conformational flexibility plays a critical role in protein function. Herein, we describe the use of time-resolved electrospray ionization mass spectrometry coupled to hydrogen-deuterium exchange for probing the rapid structural changes that drive function in ordered and disordered proteins.
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Time-resolved Electrospray IonizationHydrogen-deuterium ExchangeMass SpectrometryProtein StructureProtein DynamicsConformational FlexibilityTransient Protein ConformationsLoop RegionsMolten GlobulesIntrinsically Disordered ProteinsNeurodegenerative DisordersProtein MisfoldingProtein AggregationEnzyme Catalytic TurnoverProtein-protein InteractionsProtein-ligand InteractionsContinuous FlowTime-resolved Kinetic MixerOrthogonal Mixing
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Lento, C., Zhu, S., Brown, K. A., Knox, R., Liuni, P., Wilson, D. J. Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics. J. Vis. Exp. (122), e55464, doi:10.3791/55464 (2017).
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