Native IM-Orbitrap MS: Resolving What Was Hidden. Academic Article uri icon


  • 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.

published proceedings

  • Trends Analyt Chem

altmetric score

  • 1.25

author list (cited authors)

  • Poltash, M. L., McCabe, J. W., Shirzadeh, M., Laganowsky, A., & Russell, D. H.

citation count

  • 23

complete list of authors

  • Poltash, Michael L||McCabe, Jacob W||Shirzadeh, Mehdi||Laganowsky, Arthur||Russell, David H

publication date

  • January 2020