期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 135, 期 34, 页码 12646-12651出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja4029654
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资金
- NSF [CHE-1012622]
- Welch Foundation [F-1155]
- NIH [GM067193]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1012622] Funding Source: National Science Foundation
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.
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