Analytical Chemistry

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

Abstract

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.

Content

Thumbnail image of 2018_12_4_Surface-Induced Dissociation of Noncovalent Protein Complexes in an Extended Mass Range Orbitrap Mass Spectrometer.pdf

Supplementary material

Thumbnail image of 2018_12_4 _Supplemental_Surface-Induced Dissociation of Noncovalent Protein complexes in an Extended Mass Range Orbitrap Mass Spectrometer.pdf
2018 12 4 Supplemental Surface-Induced Dissociation of Noncovalent Protein complexes in an Extended Mass Range Orbitrap Mass Spectrometer