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Biochemistry

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

Article DOI: 10.3791/55464-v • 09:18 min • April 17th, 2017
April 17th, 2017 •
1, 1, 1, 1, 1, 1,2,3
1Department of Chemistry, York University, 2The Centre for Research in Mass Spectrometry, York University, 3The Centre for Research on Biomolecular Interactions, York University

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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 Ionization Hydrogen-deuterium Exchange Mass Spectrometry Protein Structure Protein Dynamics Conformational Flexibility Structural Biology Transient Protein Confirmations High Resolution Techniques Electrochemistry NMR Millisecond Time Scale Loop Ridges Moltinglobyals Intrinsically Disordered Proteins Neurodegenerative Disorders Misfolding Protein Aggregation Enzymes Catalytic Turnover Protein-protein Interactions Ligand Interactions Input Channel Reagents Pro Dialysis Chamber Output Channel PMM8 Block Laser Engraver
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