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Orbitrap_SciLib
Reputable Mentor II
Reputable Mentor II
Shaw JB, Li W, Holden DD, Zhang Y, Griep-Raming J, Fellers RT, Early BP, Thomas PM, Kelleher NL, Brodbelt JS.
J Am Chem Soc. 2013 Aug 28;135(34):12646-51.
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.

http://pubs.acs.org/doi/abs/10.1021/ja4029654
Department of Chemistry and Biochemistry, The University of Texas at Austin, 1 University Station A5300, Austin, Texas 78712, United States.
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