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

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 non-covalent 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 kDa 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.

Authors:
ORCiD logo; ORCiD logo; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)
Sponsoring Org.:
USDOE
OSTI Identifier:
1343174
Report Number(s):
PNNL-SA-121761
Journal ID: ISSN 0003-2700; 48903; KP1704020
DOE Contract Number:  
AC05-76RL01830
Resource Type:
Journal Article
Resource Relation:
Journal Name: Analytical Chemistry; Journal Volume: 89; Journal Issue: 1
Country of Publication:
United States
Language:
English
Subject:
Environmental Molecular Sciences Laboratory

Citation Formats

Yan, Jing, Zhou, Mowei, Gilbert, Joshua D., Wolff, Jeremy J., Somogyi, Árpád, Pedder, Randall E., Quintyn, Royston S., Morrison, Lindsay J., Easterling, Michael L., Paša-Tolić, Ljiljana, and Wysocki, Vicki H. Surface-Induced Dissociation of Protein Complexes in a Hybrid Fourier Transform Ion Cyclotron Resonance Mass Spectrometer. United States: N. p., 2017. Web. doi:10.1021/acs.analchem.6b03986.
Yan, Jing, Zhou, Mowei, Gilbert, Joshua D., Wolff, Jeremy J., Somogyi, Árpád, Pedder, Randall E., Quintyn, Royston S., Morrison, Lindsay J., Easterling, Michael L., Paša-Tolić, Ljiljana, & Wysocki, Vicki H. Surface-Induced Dissociation of Protein Complexes in a Hybrid Fourier Transform Ion Cyclotron Resonance Mass Spectrometer. United States. doi:10.1021/acs.analchem.6b03986.
Yan, Jing, Zhou, Mowei, Gilbert, Joshua D., Wolff, Jeremy J., Somogyi, Árpád, Pedder, Randall E., Quintyn, Royston S., Morrison, Lindsay J., Easterling, Michael L., Paša-Tolić, Ljiljana, and Wysocki, Vicki H. Tue . "Surface-Induced Dissociation of Protein Complexes in a Hybrid Fourier Transform Ion Cyclotron Resonance Mass Spectrometer". United States. doi:10.1021/acs.analchem.6b03986.
@article{osti_1343174,
title = {Surface-Induced Dissociation of Protein Complexes in a Hybrid Fourier Transform Ion Cyclotron Resonance Mass Spectrometer},
author = {Yan, Jing and Zhou, Mowei and Gilbert, Joshua D. and Wolff, Jeremy J. and Somogyi, Árpád and Pedder, Randall E. and Quintyn, Royston S. and Morrison, Lindsay J. and Easterling, Michael L. and Paša-Tolić, Ljiljana and Wysocki, Vicki H.},
abstractNote = {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 non-covalent 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 kDa 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.},
doi = {10.1021/acs.analchem.6b03986},
journal = {Analytical Chemistry},
number = 1,
volume = 89,
place = {United States},
year = {Tue Jan 03 00:00:00 EST 2017},
month = {Tue Jan 03 00:00:00 EST 2017}
}