- Topic: "Mass Spectrometry in Structural Biology: Surface-induced Dissociation/Ion Mobility of Protein Complexes
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- Speaker:Vicki Wysocki, Ohio State University
- Date: Monday May 11, 2015. 5:00 PM
- Time:
5:00-6:30 p.m. Vendor Show
6:30-7:30 p.m. Free Buffet-Style Dinner
7:30-7:40 p.m. Business (Election of Officers, etc)
7:40-8:45 p.m. Talk (Vicki Wysocki)
- Please RSVP to Yang Yuan Yang.Yuan@dupont.com - by Tuesday, May 5th, 2015.
An RSVP is needed to get a headcount for the served dinner.
- Place: Villanova Conference Center (Note: this is NOT on the Villanova University campus).
- Directions:http://www.acc-villanovaconferencecenter.com/villanova-conference-center-en.html
Please note: If you are using a GPS locater, please enter 629 County Line Road, Radnor, PA 19087 or Latitude 40.05 and Longitude -75.35.
- Abstract: 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 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 one of these approaches that provide lower resolution, but 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. This presentation illustrates a new approach, surface-induced dissociation/ion mobility (SID/IM) MS, for characterization of topology, intersubunit connectivity, and other structural features 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. Fragmentation to subcomplexes will be shown and the influence of charge on the fragmentation will be illustrated. In addition, SID spectra reflect well any structural changes caused by "heating" within the instrument.
- Bio:
Vicki Hopper Wysocki, B.S. in Chemistry (Western Kentucky University); Ph.D. in Chemistry (Purdue University with Professor Graham Cooks); National Research Council Postdoctoral Fellow (Naval Research Laboratory with Dr. Mark Ross). Dr. Wysocki was assistant and associate professor at Virginia Commonwealth University 1990-1995 and associate and full professor at University of Arizona (1996-2012), where she also served as department co-chair and chair. Dr. Wysocki is currently Professor and Ohio Eminent Scholar of Macromolecular Structure and Function at Ohio State University 2012- ), where she also directs the Campus Chemical Instrument Center.
Dr. Wysocki's research interests include biological applications of mass spectrometry and ion-surface interactions. In particular, Dr. Wysocki's research efforts have emphasized understanding peptide dissociation and peptide fragment ion structure and development of surface-induced dissociation/ion mobility approaches for the fragmentation of large protein complexes.
Dr. Wysocki received the American Society for Mass Spectrometry (ASMS) Research Award for young investigators and the 2009 ASMS Distinguished Contribution to Mass Spectrometry award for development of the mobile proton model. She has recently been elected to a 6 year ASMS term of office (2014-2020), serving for 2 years each as Vice President for Programs, President, and Past President. Her laboratory has been named a Waters Center of Innovation and she has recently been honored as a 2013 Purdue Outstanding Alumnus, the Michael L. Gross Award Lecturer (Nebraska), Barnett Lecturer (Northeastern University), and Conover Lecturer (Vanderbilt University). She has participated as a panel member and ad hoc reviewer for NIH, NSF, and NASA. Dr. Wysocki is also a member of the American Chemical Society and AAAS. She has served on the Editorial Board of Journal of the American Society for Mass Spectrometry and Journal of Mass Spectrometry and is currently on the Editorial or Advisory Boards of Chemical & Engineering News, Analytical Chemistry, Analyst, Mass Spectrometry Reviews, and International Journal of Mass Spectrometry.