Charge Movement and Structural Changes in the Gas-Phase Unfolding of Multimeric Protein Complexes Captured by Native Top-Down Mass Spectrometry

The extent to which noncovalent protein complexes retain native structure in the gas phase is highly dependent on experimental conditions. Energetic collisions with background gas can cause structural changes ranging from unfolding to subunit dissociation. Additionally, recent studies have highlight...

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Veröffentlicht in:	Analytical chemistry (Washington) 2020-01, Vol.92 (2), p.1788-1795
Hauptverfasser:	Zhou, Mowei, Liu, Weijing, Shaw, Jared B
Format:	Artikel
Sprache:	eng
Schlagworte:	Alcohol dehydrogenase Beta decay Chemistry Computer applications Electron capture Fragments Ionic mobility Mass spectrometry Mass spectroscopy Monitoring N-Terminus Photodissociation Protein folding Protein structure Proteins Scientific imaging Spectral signatures Spectroscopy Structural analysis Vapor phases
Online-Zugang:	Volltext
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