Differential ion mobility spectrometry (field asymmetric waveform ion mobility spectrometry (FAIMS)) is emerging as a broadly useful tool for separation of isomeric modified peptides with post-translational modifications (PTMs) attached to alternative residues. Such separations were anticipated to become more challenging for smaller PTMs and longer peptides. Here, we show that FAIMS can fully resolve localization variants involving a PTM as minuscule as methylation, even for larger peptides in the middle-down range.
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Univ North Carolina Chapel Hill, Caudill Labs, Dept Chem, Campus Box 3290, Chapel Hill, NC 27599 USAUniv North Carolina Chapel Hill, Caudill Labs, Dept Chem, Campus Box 3290, Chapel Hill, NC 27599 USA
Santiago, Brandon G.
Campbell, Matthew T.
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Univ North Carolina Chapel Hill, Caudill Labs, Dept Chem, Campus Box 3290, Chapel Hill, NC 27599 USAUniv North Carolina Chapel Hill, Caudill Labs, Dept Chem, Campus Box 3290, Chapel Hill, NC 27599 USA
Campbell, Matthew T.
Glish, Gary L.
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Univ North Carolina Chapel Hill, Caudill Labs, Dept Chem, Campus Box 3290, Chapel Hill, NC 27599 USAUniv North Carolina Chapel Hill, Caudill Labs, Dept Chem, Campus Box 3290, Chapel Hill, NC 27599 USA