Journal
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
Volume 30, Issue 9, Pages 1551-1557Publisher
SPRINGER
DOI: 10.1007/s13361-019-02238-y
Keywords
Cryogenic vibrational spectroscopy; MS2; Peptide ion fragment structure; Orbitrap; High-resolution mass spectrometry
Funding
- Air Force Office of Scientific Research (AFOSR) [FA9550-17-1-0267, FA9550-18-1-0213]
- National Science Foundation Graduate Research Fellowship [DGE-1122492]
- National Institute of Health [2T32GM008283-31]
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We describe an instrumental configuration for the structural characterization of fragment ions generated by collisional dissociation of peptide ions in the typical MS2 scheme widely used for peptide sequencing. Structures are determined by comparing the vibrational band patterns displayed by cryogenically cooled ions with calculated spectra for candidate structural isomers. These spectra were obtained in a linear action mode by photodissociation of weakly bound D-2 molecules. This is accomplished by interfacing a Thermo Fisher Scientific Orbitrap Velos Pro to a cryogenic, triple focusing time-of-flight photofragmentation mass spectrometer (the Yale TOF spectrometer). The interface involves replacement of the Orbitrap's higher-energy collisional dissociation cell with a voltage-gated aperture that maintains the commercial instrument's standard capabilities while enabling bidirectional transfer of ions between the high-resolution FT analyzer and external ion sources. The performance of this hybrid instrument is demonstrated by its application to the a(1), y(1) and z(1) fragment ions generated by CID of a prototypical dipeptide precursor, protonated L-phenylalanyl-L-tyrosine (H+-Phe-Tyr-OH or FY-H+). The structure of the unusual z(1) ion, nominally formed after NH3 is ejected from the protonated tyrosine (y(1)) product, is identified as the cyclopropane-based product is tentatively identified as a cyclopropane-based product.
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