Tandem mass spectrometry daughter experiment

Figure 9.15 Typical mass spectrometry based experiment for protein identification/characterization. (1) Proteins are fractionated by chromatography, separated by sodium dodeyl sulphate (SDS) polyacrylamide gel electrophoresis (PAGE), then excised from gel (2) the protein of interest is digested into peptide fragments, that are then (3) identified by ESI MS/MS (4) the first dimension involves molecularion analysis for peptide mass finger-printing (ql, MS only). (5) Tandem MS/MS is used when protein identification is not unambiguous, in which case parent molecular ions are activated by CID (q2) and daughter (product) ions are characterized (ToF) according to the technique of product ion scanning (illustration from Aebersold and Mann, 2003, Fig. 1).

$Figure 9.15 Typical mass spectrometry based experiment for protein identification/characterization. (1) Proteins are fractionated by chromatography, separated by sodium dodeyl sulphate (SDS) polyacrylamide gel electrophoresis (PAGE), then excised from gel (2) the protein of interest is digested into peptide fragments, that are then (3) identified by ESI MS/MS (4) the first dimension involves molecularion analysis for peptide mass finger-printing (ql, MS only). (5) Tandem MS/MS is used when protein identification is not unambiguous, in which case parent molecular ions are activated by CID (q2) and daughter (product) ions are characterized (ToF) according to the technique of product ion scanning (illustration from Aebersold and Mann, 2003, Fig. 1).$

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