Electron capture dissociation and 13C,15N depletion for deuterium localization in intact proteins after solution-phase exchange

Jay P. Charlebois, Steven M. Patrie, Neil L. Kelleher

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


For localization of deuterium atoms after solution-phase exchange with D2O, intact proteins are often digested prior to analysis by mass spectrometry (MS) and tandem MS (MS/MS). Amelioration of limitations associated with this approach (e.g., <70% sequence coverage and some D atom scrambling during MS/MS) were sought using intact proteins and two newer methods applied to tracking H/D exchange dynamics for the first time. Using 2-4-fold signal enhancements through depletion of 13C and 15N isotopes and implementing the new MS/MS technique of electron capture dissociation (ECD) yielded an increased number of c and z. ions observed (43 vs 25) for recombinant yeast ubiquitin (9.3 kDa). Initial determination of D atom content in consecutive c ion series (c4 - c7, c28, c31, c32, and c33) was demonstrated. The improved ion signal and experiment speed combined with narrower isotopic distributions markedly increases the degree of localization and feasibility of ECD-based MS/ MS after solution-phase H/D exchange.

Original languageEnglish (US)
Pages (from-to)3263-3266
Number of pages4
JournalAnalytical Chemistry
Issue number13
StatePublished - Jul 1 2003

ASJC Scopus subject areas

  • Analytical Chemistry


Dive into the research topics of 'Electron capture dissociation and <sup>13</sup>C,<sup>15</sup>N depletion for deuterium localization in intact proteins after solution-phase exchange'. Together they form a unique fingerprint.

Cite this