Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 135, Issue 34, Pages 12646-12651Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja4029654
Keywords
-
Categories
Funding
- NSF [CHE-1012622]
- Welch Foundation [F-1155]
- NIH [GM067193]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1012622] Funding Source: National Science Foundation
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available