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 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.
authors.affiliation: Department of Chemistry and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.
authors.forename: Jing
authors.identifier: 0000-0001-9901-5656
authors.initials: J
authors.lastname: Yan
authors.affiliation: Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory , Richland, Washington 99354, United States.
authors.forename: Mowei
authors.identifier: 0000-0003-3575-3224
authors.initials: M
authors.lastname: Zhou
authors.affiliation: Department of Chemistry and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.
authors.forename: Joshua D
authors.initials: JD
authors.lastname: Gilbert
authors.affiliation: Bruker Corp., Billerica, Massachusetts 01821, United States.
authors.forename: Jeremy J
authors.initials: JJ
authors.lastname: Wolff
authors.affiliation: OSU Mass Spectrometry and Proteomics Facility, The Ohio State University , Columbus, Ohio 43210, United States.
authors.forename: Árpád
authors.initials: Á
authors.lastname: Somogyi
authors.affiliation: Ardara Technologies L.P., Ardara, Pennsylvania 15615, United States.
authors.forename: Randall E
authors.initials: RE
authors.lastname: Pedder
authors.affiliation: Department of Chemistry and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.
authors.forename: Royston S
authors.initials: RS
authors.lastname: Quintyn
authors.affiliation: Department of Chemistry and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.
authors.forename: Lindsay J
authors.initials: LJ
authors.lastname: Morrison
authors.affiliation: Bruker Corp., Billerica, Massachusetts 01821, United States.
authors.forename: Michael L
authors.initials: ML
authors.lastname: Easterling
authors.affiliation: Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory , Richland, Washington 99354, United States.
authors.forename: Ljiljana
authors.initials: L
authors.lastname: Paša-Tolić
authors.affiliation: Department of Chemistry and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.
authors.forename: Vicki H
authors.initials: VH
authors.lastname: Wysocki
mesh_terms: D000619:Aminohydrolases / Q000032:analysis* / Q000378:metabolism; D002772:Cholera Toxin / Q000032:analysis*; D017357:Cyclotrons; D005583:Fourier Analysis; D013058:Mass Spectrometry; D017550:Spectroscopy, Fourier Transform Infrared; D019809:Streptavidin / Q000032:analysis*; D013499:Surface Properties
chemical_list: D002772:Cholera Toxin; D019809:Streptavidin; D000619:Aminohydrolases; C023174:toyocamycin nitrile hydrolase