Native mass spectrometry is now routinely used to measure m/z of intact protein complexes.  To gain substructure information on the complexes, an activation method in a tandem mass spectrometer is needed. Ion mobility is also used to provide information on collisional cross sections and unfolding pathways. In this presentation, the use of surface-induced dissociation (SID) coupled to ion mobility will be illustrated.  Ion mobility can be used either before or after the surface collision or two steps of surface activation can be used as shown in the figure.  Data for a number of protein-partner complexes will be presented, where the partner can be small molecule ligand, protein, DNA, or RNA.  Fragmentation to subcomplexes will be shown and the influence of charge on the fragmentation will be illustrated.  The results illustrate that substructure information is available through the surface-induced dissociation method.  In addition, SID spectra reflect well any structural changes caused by “heating” within the instrument. SID-IM-SID will be illustrated and it will be shown that substructural information is provided, along with information on charge partitioning.

SID-IM-SID: A new tool for substructure characterization of protein complexes

249th National Meeting (2015)

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