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November 1, 1994Organic Mass Spectrometry

Electrospray mass spectra of protein cations formed in basic solutions

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Authors

JBJ. C. Yves Le BlancSciex (Canada)JWJianyao WangJohnson & Johnson (United States)RGRoger GuevremontPacific Northwest National Laboratory

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Implication

Experimental mass spectrometry study reveals that peptide cation charge states correlate with base proton affinity rather than pH, highlighting gas-phase adduct dissociation mechanisms.

Key Points

  • To investigate the factors determining the charge-state distribution of gramicidin S cations electrosprayed from basic solutions containing various nitrogen bases.
  • Analyzed electrospray mass spectra of gramicidin S cations prepared in 0.2 M solutions across 18 nitrogen-containing bases.
  • Evaluated ion distributions across collision regions, including measurements performed under nominally zero collision energy conditions.
  • Relative abundances of [M + 2H]²⁺ to [M + H]⁺ ions correlated with the proton affinities of the basic additives rather than the bulk solution pH.
  • Nitrogen-base adducts desorbed into the gas phase and underwent collision-induced dissociation in the lens region, with intact adducts directly observed at zero collision energy.

Cite This Study

Blanc et al. (1994) studied this question.

synapsesocial.com/papers/6a10f9a263b25c787d9fd232https://doi.org/10.1002/oms.1210291103
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