Application of Double-beam Photodissociation in Top-down Mass Spectrometric Analysis of Ubiquitin Ions
  
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KeyWord:top-down  ion activation  infrared multiphoton dissociation(IRMPD)  ultraviolet photodissociation(UVPD)  ubiquitin  Fourier transform ion cyclotron resonance mass spectrometer(FT-ICR MS)
  
AuthorInstitution
JIAO Lu-yang,ZHANG Kai-lin,DU Meng-ying,XU Yi-cheng,LI Shu-qi,KONG Xiang-lei 1.State Key Laboratory of Elemento-Organic Chemistry,College of Chemistry,Nankai University,Tianjin ,China; 2. Life and Health Intelligent Research Institute,Tianjin University of Technology,Tianjin ,China; 3. Collaborative Innovation Center of Chemical Science and Engineering(Tianjin),Tianjin ,China
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Abstract:
      Top-down(TD) mass spectrometry(MS) could offer accurate and rich biological information at the molecular level by dissociating the complete protein ions in the gas phase. In this paper,a 3 μm infrared laser and a 210 nm ultraviolet laser were combined to introduce into the cell of an Fourier transform ion cyclotron resonance mass spectrometer(FT-ICR MS),and the top-down mass spectra for ubiquitin protein ions were obtained for the first time.The sequence coverages of the protein ions could be further optimized by optimizing the time series of two applied lasers.Experimental results showed that the dissociation could be better realized by introducing two laser beams into the ICR cell through the partial overlap in their time series.For +11 ubiquitin ions,the sequence coverages produced by the double-beam photodissociation method reached to 73%,higher than the results obtained by infrared multiphoton dissociation(IRMPD) or ultraviolet potodissociation(UVPD).For ubiquitin ions with other charge states,similar results were observed,indicating that the new method could generate richer fragmentation patterns for protein ions than UVPD or IRMPD solely and improve sequence coverages of protein ions.
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