Complete protein characterization using top-down mass spectrometry and ultraviolet photodissociation

Jared B. Shaw, Wenzong Li, Dustin D. Holden, Yan Zhang, Jens Griep-Raming, Ryan T. Fellers, Bryan P. Early, Paul M. Thomas, Neil L. Kelleher, Jennifer S. Brodbelt*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

218 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)12646-12651
Number of pages6
JournalJournal of the American Chemical Society
Volume135
Issue number34
DOIs
StatePublished - Aug 28 2013

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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