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Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
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Biochemistry
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JoVE Journal Biochemistry
Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

DOI:
10.3791/55464-v

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09:18 min

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April 17, 2017

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, , , , ,
1Department of Chemistry,York University, 2The Centre for Research in Mass Spectrometry,York University, 3The Centre for Research on Biomolecular Interactions,York University

Chapters

  • 00:05Title
  • 01:12Preparation of the Microfluidic Device
  • 05:17Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange
  • 06:51Results: Detection of Protein Structural Changes by Time-resolved ElectroSpray Ionization Hydrogen-deuterium Mass Spectrometry
  • 08:10Conclusion

Summary

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Automatic Translation

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.

Tags

Keywords: 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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