Ion mobility-mass spectrometry (IM-MS) has evolved an important tool for exploration and characterization of native, intact proteins and protein complexes, but current commercially available IM-MS instruments lack the necessary mobility and mass resolving power needed for studies of macromolecule complexes, especially membrane protein complexes. We have developed a Fourier transform-Orbitrap instrument that overcomes the duty-cycle mismatch of mobility separation (tens of ms) and Orbitrap MS (hundreds of ms). The prototype instrument utilizes a novel 1.45m periodic-focusing drift tube that is directly coupled to the HCD of the Orbitrap instrument. The IM-Orbitrap allows for first principles determination of rotationally- averaged collisional cross-sections with increased resolving power in both the mobility and mass domains. This presentation will describe this novel instrument design and results obtained from studies of biologically important protein complexes.

Fourier transform ion mobility-orbitrap for native mass spectrometry

2019 Spring National Meeting

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