Abstract

Many mass spectrometry applications make use of tandem mass spectrometry, where two stages of m/z analysis are coupled. In between the two stages of m/z analysis, an activation or reaction step is carried out to cause either structurally-informative fragmentation or structurally-characteristic reaction of the precursor ion of interest. This review focuses on the use of collisions with a surface (surface-induced dissociation, SID) as the activation method in tandem mass spectrometry, with an emphasis on SID papers published over the past four years. SID is described and compared with other activation methods. The major application focused on in this review is the structural characterization of native protein complexes, complexes kinetically trapped that retain native-like solution structures upon transfer to the gas-phase and throughout the relatively short timeframe of the mass spectrometry experiment. Other SID applications currently under investigation are also briefly described. Pioneering work on SID ...

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