Journal of the American Society for Mass Spectrometry 2015-07-01

Extensive Charge Reduction and Dissociation of Intact Protein Complexes Following Electron Transfer on a Quadrupole-Ion Mobility-Time-of-Flight MS.

Frederik Lermyte, Jonathan P Williams, Jeffery M Brown, Esther M Martin, Frank Sobott

文献索引:J. Am. Soc. Mass Spectrom. 26 , 1068-76, (2015)

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摘要

Non-dissociative charge reduction, typically considered to be an unwanted side reaction in electron transfer dissociation (ETD) experiments, can be enhanced significantly in order to reduce the charge state of intact protein complexes to as low as 1+ on a commercially available Q-IM-TOF instrument. This allows for the detection of large complexes beyond 100,000 m/z, while at the same time generating top-down ETD fragments, which provide sequence information from surface-exposed parts of the folded structure. Optimization of the supplemental activation has proven to be crucial in these experiments and the charge-reduced species are most likely the product of both proton transfer (PTR) and non-dissociative electron transfer (ETnoD) reactions that occur prior to the ion mobility cell. Applications of this approach range from deconvolution of complex spectra to the manipulation of charge states of gas-phase ions.


相关化合物

  • 乙酸铵
  • 乙醇脱氢酶
  • 谷氨酸脱氢酶
  • 丙酮酸激酶
  • 刀豆凝集素A
  • 血红蛋白

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