Electron transfer dissociation peptide selection

Zehl, M., Rand, K.D., Jensen, O.N., J0rgensen, T.J.D. (2008) Electron transfer dissociation facilitates the measurement of deuteriirm incorporation into selectively labeled peptides with single residue resolution. JAm Chem Soc, 130 (51), 17453-17459. 

In addition, new tandem mass spectrometry technologies were also among the important innovations. Apart from traditional collision-induced dissociation (CID) [89-91], a variety of activation methods (used to add energy to mass-selected ions) based on inelastic collisions and photon absorption have been widely utilized. They include IR multiphoton excitation [92,93], UV laser excitation [94—97], surface-induced dissociation (SID) [98-100], black body radiation (101, 102], thermal dissociation [103], and others. As the fragmentation of peptide/protein ions is a central topic in proteomics, there is strong interest in such novel ion dissociation methods as electron capture dissociation (ECD) [104, 105] and electron transfer dissociation [22]. These new methods can provide structural information that complements that obtained by traditional collisional activation. Also, very recently, ambient ion dissociation methods such as atmospheric pressure thermal dissociation [106] and low temperature plasma assisted ion dissociation [107] have been reported. 

As targeted ions can be selectively trapped in the ICR cell, while unwanted ions can be eliminated by the application of RF pulses, the MS" procedures in an FT-ICR-MS instrument greatly resemble those in an ion trap instrument. However, successful operation of an FT-ICR-MS instrument requires extreme low pressures in the cell. Thus, the vacuum constraints hamper the possibilities of performing CID in the FT-ICR cell [23]. This problem can be elegantly solved by the use of hybrid systems where fragmentation is performed prior to transfer of ions to the ICR cell [64, 93, 94]. Alternatively, alternative ion activation methods can be applied to induce fragmentation in the FT-ICR, such as infiared multiphoton photodissociation (IRMPD) and sustained off-resonance irradiation (SORI) [32, 33]. More recently, electron-capture (BCD) and electron-transfer dissociation (ETD) have been introduced as powerful ion dissociation tools, especially for peptides and proteins [34]. 

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