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Photodissociation Mass Spectrometry Accurately Localizes Sites of Backbone Deuteration in Peptides

preprint
submitted on 13.11.2017 and posted on 14.11.2017 by Ulrik Hvid Mistarz, Bruno Bellina, Pernille F. Jensen, Jeffery M. Brown, Perdita E. Barran, Kasper D. Rand

Hydrogen/deuterium exchange mass spectrometry (HDX-MS) is now positioned as a routinely used technique to inform on protein structure, dynamics, and interactions. Localizing the deuterium content on a single residue basis increases the spatial resolution of this technique enabling detailed structural analysis. Here we investigate the use of ultraviolet photodissociation (UVPD) at 213 nm to localize incorporated deuterium with single residue resolution in HDX-MS experiments. Using a selectively labeled peptide, we show that UVPD occurs without H/D scrambling as the peptide probe accurately retains its solution-phase deuterium labeling pattern. Our results indicate that UVPD provides an attractive alternative to electron mediated dissociation to increase the spatial resolution of the HDX-MS experiment, combining high fragmentation efficiency, high fragment ion diversity, and low charge-state dependency.

History

Topic

  • Analytical Chemistry
  • Mass Spectrometry

Email Address of Submitting Author

kasper.rand@sund.ku.dk

Email Address(es) for Other Author(s)

perdita.barran@manchester.ac.uk

Institution

University of Copenhagen

Country

Denmark

ORCID For Submitting Author

0000-0002-6337-5489

Declaration of Conflict of Interest

The authors declare no conflict of interest.

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