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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}
}
  • A new Fourier Transform Ion Cyclotron Resonance mass spectrometer (FT-ICR MS) has been constructed in our laboratory. The instrument employs surface-induced dissociation (SID) as an activation method for obtaining structural information on biomolecules in the gas phase. Tandem SID mass spectra can be acquired using either a continuous or a pulsed mode of operation. Collision energy of precursor ion is controlled by a dc offset of the ICR cell. This approach eliminates defocusing of the ion beam by the ion transfer optics as a function of ion kinetic energy and constitutes a significant improvement over our previous experimental setup. Furthermore,more » it can be easily implemented on any FT-ICR mass spectrometer. Very high signal-to-noise ratios of 200-500 were obtained in single-scan SID mass spectra of model peptides with acquisition time less than 1.1 s. Reasonable SID signal was detected in single-scan spectra with total acquisition time of only 0.3 s. The high signal-to-noise ratio and the fast acquisition time point on a potential application of SID for high-throughput studies in FT-ICR MS.« less
  • Intermediate pressure matrix assisted laser ionization (MALDI) source was constructed and interfaced with a 6T Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR MS) specially configured for surface-induced dissociation (SID) studies.
  • A new collision-induced dissociation (CID) technique based on broadband tailored noise waveform (TNW) excitation of ions stored in a linear ion trap has been developed. In comparison with the conventional sustained off-resonance irradiation (SORI) CID method commonly used in Fourier transform ion cyclotron resonance mass spectrometry, this MS/MS technique increases throughput by eliminating the long pump-down delay associated with gas introduction into the high vacuum ICR cell region. In addition, the TNW-CID method speeds spectrum acquisition since it does not require Fourier transformation, calculation of resonant frequencies and generation of the excitation waveforms. We demonstrate TNW-CID coupled with on-line capillarymore » reverse phase liquid chromatography separations for identification of peptides. The experimental results are compared with data obtained using conventional quadrupole ion trap MS/MS and SORI-CID MS/MS in an ICR cell.« less
  • A fourier transform ion cyclotron resonance (FTICR) mass spectrometer has been used to trap individual multiply charged ions of several high molecular weight polymers, including poly(ethylene oxide), sodium poly(styrene sulfonate), and the protein bovine serum albumin. Detection of these ions is performed with the nondestructive method distinctive of FTICR, which also allows remeasurement of the same ion or ion population over several hours. For the determination of the charge states (and hence the masses) of individual ions, a new scheme was developed on the basis of the observation of the stepwise m/z shifts that results from charge exchange reactions ormore » adduction of a substance of known mass. A novel technique for mass determination of individual ions has been made possible with the observation of cyclotron frequency shifts during the time-domain acquisition period. This time-resolved ion correlation (TRIC) technique allows reactant and product ions to be correlated with confidence and provides the basis for simultaneously studying a moderate number of ions. In this work, a range of observations related to the detection and measurement of individual ions is presented, as are examples of mass determinations of individual ions performed by utilizing the TRIC technique. 47 refs., 9 figs., 2 tabs.« less