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- Faraday Lecture
Vicki Hopper Wysocki, Ph.D., Ohio Eminent Scholar Faculty, Professor, Department of Chemistry and Biochemistry, Ohio State University
“Native MS in Structural Biology”
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. However, other emerging biophysical methods that provide lower resolution structural 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 higher throughput on low sample amounts. 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 (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. Data for a number of protein-partner complexes are under investigation, where the partner can be small molecule ligand, protein, DNA, or RNA.
View meeting dates and speaker information.
October 2, 2017
November 6, 2017
December Joint Meeting – TBA
January 8, 2018
February 5, 2018
Feb 25 – Mar 1 – Pittcon 2018
April 4 – Former Chair Night
May 14 – Awards Banquet
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Call for nominations are open for the Pittsburgh Analytical Chemistry Award and the Pittsburgh Conference Achievement Award.