Characterization of the overall topology and inter-subunit contacts of protein complexes, and their assembly/disassembly and unfolding pathways, is critical because protein complexes regulate key biological processes, including processes important in understanding and controlling disease. Conventional structural biology methods such as X-ray crystallography and nuclear magnetic resonance provide high-resolution information on the structures of protein complexes and are the gold standards in the field. However, other emerging biophysical methods are also important. Native mass spectrometry is an approach that can provide critical structural information with high throughput. The power of native MS increases when coupled to ion mobility (IM-MS), a technique that measures rotationally averaged collisional cross sections and thus direct information on conformational changes, or to high resolution mass spectrometry which can provide accurate mass measurements of complexes and their ligands. . This presentation illustrates the use of surface-induced dissociation/ion mobility (SID/IM) MS and surface-induced dissociation/high resolution (ICR) MS for characterization of topology, intersubunit connectivity, and other structural features (degree of unfolding) of multimeric protein complexes. Data for a number of protein-partner complexes will be presented, where the partner can be small molecule ligand, protein, DNA, or RNA.

Insights into protein complex structure from surface-induced dissociation MS coupled to ion mobility or high resolution analysis

251st National Meeting (2016)

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