title: Surface-induced dissociation shows potential to be more informative than collision-induced dissociation for structural studies of large systems.
abstract: 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.
authors.affiliation: Department of Chemistry, Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, Arizona 857-0041, USA. vwysocki@email.arizona.edu
authors.forename: Vicki H
authors.initials: VH
authors.lastname: Wysocki
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Jones
authors.forename: Asiri S
authors.initials: AS
authors.lastname: Galhena
authors.forename: Anne E
authors.initials: AE
authors.lastname: Blackwell
mesh_terms: D000818:Animals; D006801:Humans; D046912:Multiprotein Complexes / Q000737:chemistry*; D011487:Protein Conformation; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D013499:Surface Properties
chemical_list: D046912:Multiprotein Complexes