1. Surface-Induced Dissociation of Protein Complexes in a Hybrid Fourier Transform Ion Cyclotron Resonance Mass Spectrometer.
- Author
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Yan, Jing, Zhou, Mowei, Gilbert, Joshua D., Wolff, Jeremy J., Somogyi, A?rpa?d, Pedder, Randall E., Quintyn, Royston S., Morrison, Lindsay J., Easterling, Michael L., Pas?a-Tolic?, Ljiljana, and Wysocki, Vicki H.
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DISSOCIATION (Chemistry) , *FOURIER transform spectrometers , *ION cyclotron resonance spectrometry , *PROTEIN analysis , *COMPLEX compounds - Abstract
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. [ABSTRACT FROM AUTHOR]
- Published
- 2017
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