Journal article

Protonation isomers of highly charged protein ions can be separated in FAIMS-MS

J Diana Zhang, Micah T Donor, Amber D Rolland, Michael G Leeming, Huixin Wang, Adam J Trevitt, KM Mohibul Kabir, James S Prell, William A Donald

International Journal of Mass Spectrometry | ELSEVIER | Published : 2020

Abstract

High-field asymmetric waveform ion mobility spectrometry-mass spectrometry (FAIMS-MS) can resolve over an order of magnitude more conformers for a given protein ion than alternative methods. Such an expansion in separation space results, in part, from protein ions with masses of >29 kDa undergoing dipole alignment in the high electric field of FAIMS, and the resolution of ions that adopt pendular vs free rotor states. In this study, FAIMS-MS, collision-induced dissociation (CID), and travelling wave (TW) IMS-MS were used to investigate the pendular and free rotor states of protonated carbonic anhydrase II (CAII, 29 kDa). The electrospray ionization additive 1,2-butylene carbonate was used to..

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University of Melbourne Researchers

Grants

Awarded by Australian Research Council


Funding Acknowledgements

AJT and WAD acknowledge support from the Australian Research Council (DP200100065). KMMK acknowledges support from the Australian Research Council (DE190100986). We thank the Bioanalytical Mass Spectrometry Facility at UNSW Sydney for access to some instrumentation.