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• W2798508788 abstract "A database of ion-neutral collision cross-sections for singly-charged peptide ions is presented. The peptides included in the database were generated by enzymatic digestion of known proteins using three different enzymes, resulting in peptides that differ in terms of amino acid composition as well as N-terminal and C-terminal residues. The ion-neutral collision crosssections were measured using ion mobility (IM) spectrometry that is directly coupled to a time-of-flight (TOF) mass spectrometer. The ions were formed by a matrix-assisted laser desorption ionization (MALDI) ion source operated at pressures (He bath gas) of 2 to 3 torr. The majority (63%) of the peptide ion collision cross-sections correlate well with structures that are best described as charge-solvated globules, but a significant number of the peptide ions exhibit collision cross-sections that are significantly larger or smaller than the average, globular mobility-mass correlation. Of the peptide ions having larger than average collision crosssections, 71% are derived from trypsin digestion (C-terminal Arg or Lys residues) and most of the peptide ions that have smaller (than globular) collision cross-sections are derived from pepsin digestion (90%). (J Am Soc Mass Spectrom 2007, 18, 1232–1238) © 2007 American Society for Mass Spectrometry" @default.
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• W2798508788 date "2007-01-01" @default.
• W2798508788 modified "2023-09-27" @default.
• W2798508788 title "FOCUS: FROM MOBILITIES TO PROTEOMES A Collision Cross-Section Database of Singly-Charged Peptide Ions" @default.
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