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Issue 10, 2018
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Tandem trapped ion mobility spectrometry

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There is currently a strong interest in the use of ion mobility spectrometry-mass spectrometry (IMS-MS) instrumentation for structural biology. In these applications, momentum transfer cross sections derived from IMS-MS measurements are used to reconstruct the three-dimensional analyte structure. Recent reports indicate that additional structural information can be extracted from measuring changes in cross sections in response to changes of the analyte structure. To further this approach, we constructed a tandem trapped IMS analyser (TIMS-TIMS) and incorporated it in a QqTOF mass spectrometer. TIMS-TIMS is constructed by coupling two TIMS analysers via an “interface region” composed of two apertures. We show that peptide oligomers (bradykinin) and native-like protein (ubiquitin) ions can be preserved through the course of an experiment in a TIMS-TIMS analyser. We demonstrate the ability to collisionally-activate as well as to trap mobility-selected ions, followed by subsequent mobility-analysis. In addition to inducing conformational changes, we show that we can fragment low charge states of ubiquitin at >1 mbar between the TIMS analysers with significant sequence coverage. Many fragment ions exhibit multiple features in their TIMS spectra, which means that they may not generally exist as the most stable isomer. The ability of TIMS-TIMS to dissociate mobility-selected protein ions and to measure the cross sections of their fragment ions opens new possibilities for IMS-based structure elucidation.

Graphical abstract: Tandem trapped ion mobility spectrometry

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Publication details

The article was received on 19 Dec 2017, accepted on 20 Mar 2018 and first published on 23 Mar 2018

Article type: Paper
DOI: 10.1039/C7AN02054F
Citation: Analyst, 2018,143, 2249-2258
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    Tandem trapped ion mobility spectrometry

    F. C. Liu, M. E. Ridgeway, M. A. Park and C. Bleiholder, Analyst, 2018, 143, 2249
    DOI: 10.1039/C7AN02054F

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