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Surface-Induced Dissociation of Noncovalent Protein Complexes in an Extended Mass Range Orbitrap Mass Spectrometer

preprint
submitted on 04.12.2018, 12:23 and posted on 05.12.2018, 15:32 by Zachary VanAernum, Joshua D. Gilbert, Mikhail E. Belov, Alexander A. Makarov, Stevan R. Horning, Vicki H. Wysocki
Herein we demonstrate the first adaptation of surface-induced dissociation in a modified high-mass range, high-resolution Orbitrap mass spectrometer. The SID device was designed to be installed in the Q-Exactive series of Orbitrap mass spectrometers with minimal disruption of standard functions. The performance of the SID-Orbitrap instrument has been demonstrated with several protein complex and ligand-bound protein complex systems ranging from 53 to 336 kDa. We also address the effect of ion source temperature on native protein-ligand complex ions as assessed by SID. Results are consistent with previous findings on quadrupole time-of-flight instruments and suggest that SID coupled to high-resolution MS is well-suited to provide information on the interface interactions within protein complexes and ligand-bound protein complexes.

Funding

IDBR: Type A. High-Performance Surface-induced Dissociation MS/MS

Directorate for Biological Sciences

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Resource for Native Mass Spectrometry Guided Structural Biology

National Institute of General Medical Sciences

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History

Email Address of Submitting Author

vanaernum.2@osu.edu

Institution

The Ohio State University

Country

United States of America

ORCID For Submitting Author

0000-0002-0956-3956

Declaration of Conflict of Interest

M.E.B., A.A.M, and S.R.H. are employees of Thermo Fisher Scientific. The authors declare no additional conflicts of interest.

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