Surface-Induced Dissociation of Protein Complexes in a Hybrid Fourier Transform Ion Cyclotron Resonance Mass Spectrometer

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• 作者：Jing YanMowei Zhou ; Joshua D. GilbertJeremy J. Wolff ; Árpád Somogyi ; Randall E. Pedder ; Royston S. Quintyn ; Lindsay J. Morrison ; Michael L. Easterling ; Ljiljana Paša-Tolić ; Vicki H. Wysocki
• 刊名：Analytical Chemistry
• 出版年：2017
• 出版时间：January 3, 2017
• 年：2017
• 卷：89
• 期：1
• 页码：895-901
• 全文大小：462K
• ISSN：1520-6882

文摘

Mass spectrometry continues to develop as a valuable tool in the analysis of proteins and protein complexes. In protein complex mass spectrometry studies, surface-induced dissociation (SID) has been successfully applied in quadrupole time-of-flight (Q-TOF) instruments. SID provides structural information on noncovalent protein complexes that is complementary to other techniques. However, the mass resolution of Q-TOF instruments can limit the information that can be obtained for protein complexes by SID. Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) provides ultrahigh resolution and ultrahigh mass accuracy measurements. In this study, an SID device was designed and successfully installed in a hybrid FT-ICR instrument in place of the standard gas collision cell. The SID-FT-ICR platform has been tested with several protein complex systems (homooligomers, a heterooligomer, and a protein–ligand complex, ranging from 53 to 85 kDa), and the results are consistent with data previously acquired on Q-TOF platforms, matching predictions from known protein interface information. SID fragments with the same m/z but different charge states are well-resolved based on distinct spacing between adjacent isotope peaks, and the addition of metal cations and ligands can also be isotopically resolved with the ultrahigh mass resolution available in FT-ICR.