Travelling wave ion mobility mass spectrometry studies of protein structure: Biological significance and comparison with X-ray crystallography and nuclear magnetic resonance spectroscopy measurements

Charlotte A. Scarff, Konstantinos Thalassinos, Gillian R. Hilton, James Scrivens

    Research output: Contribution to journalArticle

    119 Citations (Scopus)

    Abstract

    The three-dimensional conformation of a protein is central to its biological function. The characterisation of aspects of three-dimensional protein structure by mass spectrometry is an area of much interest as the gas-phase conformation, in many instances, can be related to that of the solution phase. Travelling wave ion mobility mass spectrometry (TWIMS) was used to investigate the biological significance of gas-phase protein structure. Protein standards were analysed by TWIMS under denaturing and near-physiological solvent conditions and cross-sections estimated for the charge states observed. Estimates of collision cross-sections were obtained with reference to known standards with published cross-sections. Estimated cross-sections were compared with values from published X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy structures. The cross-section measured by ion mobility mass spectrometry varies with charge state, allowing the unfolding transition of proteins in the gas phase to be studied. Cross-sections estimated experimentally for proteins studied, for charge states most indicative of native structure, are in good agreement with measurements calculated from published X-ray and NMR structures. The relative stability of gas-phase structures has been investigated, for the proteins studied, based on their change in cross-section with increase in charge. These results illustrate that the TWIMS approach can provide data on three-dimensional protein structures of biological relevance.

    Original languageEnglish
    Pages (from-to)3297-3304
    Number of pages8
    JournalRapid Communications in Mass Spectrometry
    Volume22
    Issue number20
    DOIs
    Publication statusPublished - 30 Oct 2008

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