The Role of Electron Transfer Dissociation in Modern Proteomics

In the nearly fifteen years since electron transfer dissociation (ETD) was introduced,1 bioanalytical mass spectrometry (MS) and MS-driven proteomics have continued to develop as the premier tools for characterizing proteome composition, structure, and function.2 The new era of proteomics has focused on throughput, sampling depth, and reproducibility – often relying on traditional collision-based dissociation because of its speed and ease of implementation.3–5 That said, the development of alternative dissociation methods remains an active field in proteome research, offering complementary analyses to collisional activation and valuable insights for analytes that can be intractable with traditional methods.6 Because of its applicability to a wide range of biomolecules and its compatibility with a variety of instrument platforms, ETD is among the most prominent of these alternative approaches. Concentrating on developments in the last five years, this review examines the role ETD plays in modern proteomic ...