2013/05/22 by Jared Shaw, Wenzong Li, Dustin D. Holden +7 · 6 citations
Chemistry · Materials Science · #Advanced Proteomics Techniques and Applications #Biochemistry #Characterization (materials science) #Chemistry #Chromatography #Dissociation (chemistry) #Electron-capture dissociation #Electron-transfer dissociation #Enzyme Structure and Function #Fragmentation (computing) #Gene #Mass Spectrometry Techniques and Applications #Mass spectrometry #Nanotechnology #Optoelectronics #Orbitrap #Photochemistry #Photodissociation #Protein mass spectrometry #Proteomics #Tandem mass spectrometry #Top-down proteomics #Ultraviolet
paper · doi:10.1021/ja4029654
openalex publication_date 2013/05/22 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
The top-down approach to proteomics offers compelling advantages due to the potential to provide complete characterization of protein sequence and post-translational modifications. Here we describe the implementation of 193 nm ultraviolet photodissociation (UVPD) in an Orbitrap mass spectrometer for characterization of intact proteins. Near-complete fragmentation of proteins up to 29 kDa is achieved with UVPD including the unambiguous localization of a single residue mutation and several protein modifications on Pin1 (Q13526), a protein implicated in the development of Alzheimer's disease and in cancer pathogenesis. The 5 ns, high-energy activation afforded by UVPD exhibits far less precursor ion-charge state dependence than conventional collision- and electron-based dissociation methods.