Gaseous apomyoglobin ion dissociation in a quadrupole ion trap: [M + 2H] 2+ -[M + 21H] 21+ 1 1Prepared for submission to the International Journal of Mass Spectrometry in honor of Prof. R. Graham Cooks on the occasion of his 60th birthday
| Autor: | Kelly A. Newton, J. Mitchell Wells, Paul A. Chrisman, Scott A. McLuckey, Gavin E. Reid |
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| Rok vydání: | 2001 |
| Předmět: |
Collision-induced dissociation
Electron-capture dissociation Chemistry Analytical chemistry Protonation Condensed Matter Physics Tandem mass spectrometry Dissociation (chemistry) Ion Crystallography Physics::Plasma Physics Infrared multiphoton dissociation Physical and Theoretical Chemistry Quadrupole ion trap Instrumentation Spectroscopy |
| Zdroj: | International Journal of Mass Spectrometry. 212:359-376 |
| ISSN: | 1387-3806 |
| DOI: | 10.1016/s1387-3806(01)00485-7 |
| Popis: | The dissociation of the multiply protonated ions of apomyoglobin ranging in charge from [M + 2H] 2+ to [M + 21H] 21+ have been studied using collisional activation and ion/ion reactions in a quadrupole ion trap. A variety of collisional activation conditions were explored for each charge state to determine optimal conditions for yielding the highest quality product ion spectra. Product ion spectra for charge states greater than [M + 6H] 6+ were acquired using both on-resonance and off-resonance collisional activation, with on-resonance activation conditions providing the highest quality spectra. Product ion spectra for the lowest charge states could only be acquired using on-resonance collisional activation. The lowest charge states show a high propensity for losses of small molecules, as well as a number of favored amide bond cleavages, such as fragmentation C-terminal to aspartic acid residues. A novel, dominant cleavage between adjacent lysine-histidine residues was also observed, particularly for charge states higher than [M + 6H] 6+ . The largest number of structurally informative fragments, corresponding to b-type or y-type product ions, were produced from the intermediate charge states of [M + 10H] 10+ to [M + 14H] 14+ . The product ion spectra for the charge states of [M + 15H] 15+ and higher were dominated by the y 151 ion, which appeared to be related to protonation of the N-terminus and, possibly, a secondary structure effect. The overall charge state dependent fragmentation behavior of apomyoglobin ions parallels that of other protein ions studied to date using a quadrupole ion trap in that the most extensive structural information is yielded by parent ions of intermediate charge states. This behavior is consistent with these intermediate charge states either being comprised of a diversity of parent ion structures, having a relatively high degree of proton mobility, or a combination of both. |
| Databáze: | OpenAIRE |
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