Mass spectrometry methods for studying structure and dynamics of biological macromolecules.

■ CONTENTS Hydrogen/Deuterium Exchange 214 Fundamentals 214 Proteolytic Digestion-LC/MS 215 Characterization of Binding Interactions 216 HDX/MS of Intrinsically Disordered Proteins 216 Membrane Protein HDX/MS 217 Pulsed HDX/MS 217 Cytotoxic Protein Aggregates Studied by HDX/ MS 218 Application of HDX/MS to Protein Therapeutics 218 Single Amide Resolution 218 HDX/MS with Electron-Based Fragmentation 218 Covalent Labeling 220 General Considerations 220 Hydroxyl Radical Labeling 220 Covalent Cross-Linking 222 ESI Charge State Distributions 222 ESI Mechanism for Folded Proteins 222 CID of Multiprotein Complexes 223 ESI Mechanism for Unfolded Proteins 223 “Supercharging” and Related Phenomena 224 Native Mass Spectrometry and Ion Mobility Spectrometry 224 Preservation of Native-Like Structures in the Gas Phase 224 Ion Mobility Spectrometry and Other Techniques for Probing Gas Phase Structures 224 Protein−Protein Complexes 225 Other Types of Noncovalent Assemblies 225 Concluding Remarks 227 Author Information 227 Corresponding Author 227 Notes 227 Biographies 227 Acknowledgments 227 References 227

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