Abstract
High field asymmetric waveform ion mobility spectrometry (FAIMS) is well-established as a tool for separating peptide isomers (sequence inversions and post-translationally modified localization variants). Here, we demonstrate the FAIMS is able to differentiate cis and trans isomers of polyproline. Polyproline assumes an all-cis conformation—the PPI helix—in 1-propanol, and an all-trans conformation—the PPII helix—in aqueous solutions. Differentiation of these conformers may be achieved both through use of a cylindrical FAIMS device and a miniaturized ultrahigh field planar FAIMS device.
Original language | English |
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Pages (from-to) | 2071–2074 |
Journal | Journal of the American Society for Mass Spectrometry |
Volume | 27 |
Issue number | 12 |
Early online date | 4 Oct 2016 |
DOIs | |
Publication status | Published - Dec 2016 |
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Separation of cis and trans isomers of polyproline by FAIMS mass spectrometry
Cooper, H. (Creator), University of Birmingham, 2016
DOI: 10.25500/eData.bham.00000168
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