Collisions of Large Non-Covalent Complexes into Surfaces : An MS-Based Structural Biology Tool

Event details

Date	22.09.2016
Hour	16:30 › 17:30
Speaker	Prof. Vicki Wysocki Ohio State University Department of Chemistry and Biochemistry
Location	CH G1 495
Category	Conferences - Seminars

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, nuclear magnetic resonance, and cryo-electron microscopy provide high-resolution information on the structures of protein complexes and are the gold standards in the field. However, other emerging biophysical methods that provide lower resolution data (e.g. stoichiometry and subunit connectivity) on the structures of the protein complexes are also important. Native mass spectrometry is an approach that provides critical structural information with high throughput on low sample amounts. The power of native MS increases when coupled to collisions of the large non-covalent complexes with a target surface to cause dissociation of the complex into subcomplexes. Additional increases in information are seen by coupling the surface collision experiment with ion mobility (IM-MS), a technique that measures rotationally averaged collisional cross sections and thus direct information on conformational changes, or high resolution mass spectrometry (HRMS). This presentation illustrates surface-induced dissociation/ion mobility (SID/IM) MS and SID/HRMS for characterization of topology, intersubunit connectivity, and other structural features of multimeric protein complexes.