Electron capture dissociation tandem mass spectrometry using

Stevens, S.M., Rauniyar, N., Prokai, L. (2007) Characterization of 4-hydroxy-2-nonenal-modified peptides by hquid chromatography-tandem mass spectrometry using data-dependent acquisition neutral loss-driven MS versus neutral loss-driven electron capture dissociation. Journal of Mass Spectrometry, 42,1599-1605. 

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. 

In situations where it is desirable to preferentially form analyte ions of higher charge state—for example, to obtain more reactive precursors for tandem mass spectrometry experiments or to improve the efficiency of electron capture in either electron capture dissociation (ECD) or electron transfer dissociation (ETD) experiments—then the use of narrow diameter capillaries is recommended. Conversely, if lower charge states are desirable, such as singly charged small molecule precursor ions that present more straightforward spectral interpretation, then wider diameter capillaries are preferable. ... 

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