Ion mobility mass spectrometry of proteins in a modified commercial mass spectrometer

K. Thalassinos, S. E. Slade, K. R. Jennings, James Scrivens, K. Giles, J. Wildgoose, J. Hoyes, R. H. Bateman, M. T. Bowers

    Research output: Contribution to journalArticlepeer-review

    80 Citations (Scopus)

    Abstract

    Ion mobility has emerged as an important technique for determining biopolymer conformations in solvent free environments. These experiments have been nearly exclusively performed on home built systems. In this paper we describe modifications to a commercial high performance mass spectrometer, the Waters UK "Ultima" Q-Tof, that allows high sensitivity measurement of peptide and protein cross sections. Arrival time distributions are obtained for a series of peptides (bradykinin, LHRH, substance P, bombesin) and proteins (bovine and equine cytochrome c, myoglobin, α-lactalbumin) with good agreement found with literature cross sections where available. In complex ATD's, mass spectra can be obtained for each feature confirming assignments. The increased sensitivity of the commercial instrument is retained along with the convenience of the data system, crucial features for analysis of protein misfolding systems.

    Original languageEnglish
    Pages (from-to)55-63
    Number of pages9
    JournalInternational Journal of Mass Spectrometry
    Volume236
    Issue number1-3
    DOIs
    Publication statusPublished - 1 Aug 2004

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