Journal
TRAC-TRENDS IN ANALYTICAL CHEMISTRY
Volume 124, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.trac.2019.05.035
Keywords
Ion mobility-mass spectrometry; Native mass spectrometry; Intact protein complexes; Protein-ligand interactions; Fourier transform-ion mobility; High resolution mass spectrometry; Periodic focusing drift tube ion mobility; Orbitrap mass spectrometer; Ion mobility; Membrane protein
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Funding
- National Science Foundation [CHE-1707675]
- National Institutes of Health [DP2GM123486, R01GM121751, P41GM128577]
- MDS Sciex Professorship
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Native ion mobility-mass spectrometry (IM-MS) is an emerging biophysical approach to probe the intricate details of protein structure and function. The instrument design enables measurements of accurate first-principle determinations of rotationally-averaged ion-neutral collision cross sections coupled with high-mass, high-resolution mass measurement capabilities of Orbitrap MS. The inherent duty-cycle mismatch between drift tube IM and Orbitrap MS is alleviated by operating the drift tube in a frequency modulated mode while continuously acquiring mass spectra with the Orbitrap MS. Fourier transform of the resulting time-domain signal, i.e., ion abundances as a function of the modulation frequency, yields a frequency domain spectrum that is then converted (s(-1) to s) to IM drift time. This multiplexed approach allows for a duty-cycle of 25% compared to <1% for traditional pulse-and-wait IM-ToF-MS. Improvements in mobility and mass resolution of the IM-Orbitrap allows for accurate analysis of intact protein complexes and the possibility of capturing protein dynamics. (C) 2019 Elsevier B.V. All rights reserved.
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