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

Yan, Jing; Zhou, Mowei; Gilbert, Joshua D.; Wolff, Jeremy J.; Somogyi, Arpad; Pedder, Randall E.; Quintyn, Royston S.; Morrison, Lindsay J.; Easterling, Michael L.; Pasa-Tolic, Ljiljana; Wysocki, Vicki H.

doi:10.1021/acs.analchem.6b03986

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

Journal Article · Fri Dec 02 00:00:00 EST 2016 · Analytical Chemistry

DOI:https://doi.org/10.1021/acs.analchem.6b03986· OSTI ID:1418480

^[1];

^[2]; Gilbert, Joshua D. ^[1]; Wolff, Jeremy J. ^[3]; Somogyi, Arpad ^[4]; Pedder, Randall E. ^[5]; Quintyn, Royston S. ^[1]; Morrison, Lindsay J. ^[1]; Easterling, Michael L. ^[3]; Pasa-Tolic, Ljiljana ^[2]; Wysocki, Vicki H. ^[1]

The Ohio State Univ., Columbus, OH (United States). Dept. of Chemistry and Biochemistry
Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)
Bruker Corp., Billerica, MA (United States)
The Ohio State Univ., Columbus, OH (United States). OSU Mass Spectrometry and Proteomics Facility
Ardara Technologies L.P., Ardara, PA (United States)

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. Here 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. Lastly, 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.

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Research Organization:: Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)

Sponsoring Organization:: National Science Foundation (NSF); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH)

OSTI ID:: 1418480

Journal Information:: Analytical Chemistry, Vol. 89, Issue 1; ISSN 0003-2700

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 21 works

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Surface Induced Dissociation Coupled with High Resolution Mass Spectrometry Unveils Heterogeneity of a 211 kDa Multicopper Oxidase Protein Complex Zhou, Mowei; Yan, Jing; Romano, Christine A. Journal of The American Society for Mass Spectrometry, Vol. 29, Issue 4 https://doi.org/10.1007/s13361-017-1882-x	journal	January 2018
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