Surface-induced dissociation shows potential to be more informative than collision-induced dissociation for structural studies of large systems.
The ability to preserve noncovalent, macromolecular assemblies intact in the gas phase has paved the way for mass spectrometry to characterize ions of increasing size and become a powerful tool in the field of structural biology. Tandem mass spectrometry experiments have the potential to expand the capabilities of this technique through the gas-phase dissociation of macromolecular complexes, but collisions with small gas atoms currently provide very limited fragmentation. One alternative for dissociating large ions is to collide them into a surface, a more massive target. Here, we demonstrate the ability and benefit of fragmenting large protein complexes and inorganic salt clusters by surface-induced dissociation (SID), which provides more extensive fragmentation of these systems and shows promise as an activation method for ions of increasing size.
Wysocki
Vicki H
VH
Department of Chemistry, Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, Arizona 857-0041, USA. vwysocki@email.arizona.edu
Jones
Christopher M
CM
Galhena
Asiri S
AS
Blackwell
Anne E
AE
D000818:Animals; D006801:Humans; D046912:Multiprotein Complexes / Q000737:chemistry*; D011487:Protein Conformation; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D013499:Surface Properties
D046912:Multiprotein Complexes