Field Asymmetric Waveform Ion Mobility Spectrometry Studies of Proteins: Dipole Alignment in Ion Mobility Spectrometry?
Approaches to characterization and separation of ions involving their mobilities in gases were developed since 1960-s. Conventional ion mobility spectrometry (IMS) measures the absolute mobility and the field asymmetric waveform IMS (FAIMS) exploits the difference between mobilities at high and low electric fields. However, all previous work was based on the orientationally averaged cross-sections Ωavg between ions and buffer gas molecules. Virtually all large ions are electric dipoles that will be oriented by a sufficiently strong electric field. At typical FAIMS conditions, that must happen for dipole moments > ~400 Debye, found for many macroions including most proteins above ~30 kDa. Mobilities of aligned dipoles depend on directional cross-sections Ωdir (rather than Ωavg), which should have a major effect on FAIMS separation parameters. Here we study the FAIMS behavior of ESI-generated ions for ten proteins up to ~70 kDa. Those above 29 kDa exhibit a strong increase of mobility at high field, which is consistent with predicted ion dipole alignment. This effect expands the FAIMS peak capacity by an order of magnitude, allowing separation of up to ~102 distinct protein conformers and revealing information about Ωdir and ion dipole moment that is of potential utility for structural characterization. Possible means to extend the dipole alignment to smaller ions are discussed.
- Research Organization:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 894461
- Report Number(s):
- PNNL-SA-49341; TRN: US200701%%467
- Journal Information:
- Journal of Physical Chemistry B, 110(43):21966-21980, Journal Name: Journal of Physical Chemistry B, 110(43):21966-21980
- Country of Publication:
- United States
- Language:
- English
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