“Fast excitation” cid in a quadrupole ion trap mass spectrometer
Collision-induced dissociation (CID) in a quadrupole ion trap mass spectrometer is usually performed by applying a small amplitude excitation voltage at the same secular frequency as the ion of interest. Here we disclose studies examining the use of large amplitude voltage excitations (applied for s...
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Veröffentlicht in: | Journal of the American Society for Mass Spectrometry 2003-07, Vol.14 (7), p.785-789 |
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Sprache: | eng |
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Zusammenfassung: | Collision-induced dissociation (CID) in a quadrupole ion trap mass spectrometer is usually performed by applying a small amplitude excitation voltage at the same secular frequency as the ion of interest. Here we disclose studies examining the use of large amplitude voltage excitations (applied for short periods of time) to cause fragmentation of the ions of interest. This process has been examined using leucine enkephalin as the model compound and the motion of the ions within the ion trap simulated using ITSIM. The resulting fragmentation information obtained is identical with that observed by conventional resonance excitation CID. “Fast excitation” CID deposits (as determined by the intensity ratio of the a
4/b
4 ion of leucine enkephalin) approximately the same amount of internal energy into an ion as conventional resonance excitation CID where the excitation signal is applied for much longer periods of time. The major difference between the two excitation techniques is the higher rate of excitation (gain in kinetic energy) between successive collisions with helium atoms with “fast excitation” CID as opposed to the conventional resonance excitation CID. With conventional resonance excitation CID ions fragment while the excitation voltage is still being applied whereas for “fast excitation” CID a higher proportion of the ions fragment in the ion cooling time following the excitation pulse. The fragmentation of the (M + 17H)
17+ of horse heart myoglobin is also shown to illustrate the application of “fast excitation” CID to proteins. |
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ISSN: | 1044-0305 1879-1123 |
DOI: | 10.1016/S1044-0305(03)00326-X |