Mass spectrometry has undergone explosive change over the past three decades, changing from a technique used for characterization of volatile molecules to a technique that can characterize a wide variety of sample types.  Of particular interest in recent years is the use of mass spectrometry for the characterization of molecular assemblies.  Protein-ligand, protein-protein, and protein-DNA(RNA) complexes can now be examined by mass spectrometry.  In this presentation, a number of examples will be presented that illustrate the types of structural information obtained by a combination of surface-induced dissociation with ion mobility.  Dissociation behavior for a variety of different stoichiometries and binding partners will be illustrated.  The influence of charge state and topology on fragmentation patterns will also be illustrated for a number of different complexes.  The data show that protein complexes that collide with a surface can retain their initial collisional cross section in circumstances where collisions with a gas lead to protein unfolding.  Surface collisions lead to informative fragmentation for systems that do not fragment by gas collisions and for systems for which substructure information is not provided by gas collisions.

Surface-induced dissociation coupled to ion mobility for characterization of noncovalent complexes

246th National Meeting (2013)

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