March 2008 Meeting Announcement, Delaware Valley Mass Spectrometry Discussion Group
NOTE: Meeting is on Tuesday March 11, 2008. Room 2010, Bartley Hall
- Topic: "Hydrogen/Deuterium Exchange Mass Spectrometry for the Analysis of Protein Conformation and Dynamics
- Speaker: John R. Engen, Northeastern University
- Date: Tuesday, March 11, 2008. 6:30 PM
- Time: Social Hour: 6:30 PM.
Talk: 7:30 PM.
Please RSVP to Christopher Petucci PETUCCC@wyeth.com by Thursday March 6th.
- Place: Department of Chemistry, Villanova University (room 2010, Bartley)
Mass spectrometry can be applied to a variety of analytical problems. One of the less utilized areas of mass spectrometry is the analysis of protein conformation and dynamics. By labeling protein molecules under physiological conditions, either covalently or non-covalently, information can be captured about their folded state. Hydrogen exchange methods non-covalently label the backbone amide hydrogens of proteins with deuterium and the location and magnitude of the labeling can then be determined with mass spectrometry. Several examples of the utility of hydrogen exchange methods will be shown for viral accessory proteins and proteins of importance to the biotechnology and pharmaceutical industries.
John R. Engen is an Associate Professor of Chemistry & Chemical Biology at Northeastern University in Boston. He also holds the position of Faculty Fellow in the Barnett Institute of Chemical and Biological Analysis. Prior to coming to Northeastern, he was an Assistant Professor of Chemistry, Biochemistry and Molecular Biology at the University of New Mexico in Albuquerque and a Member of the University of New Mexico Cancer Center. Professor Engen holds two BS degrees (molecular biology and biochemistry) from Union College and a PhD in Chemistry from the University of Nebraska (working with David L. Smith). He completed postdoctoral work at the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany and at Los Alamos National Laboratory. He is a Fellow of the European Molecular Biology Organization (EMBO).
Professor Engen has become a recognized expert in the area of understanding proteins and protein conformation with mass spectrometry. He uses hydrogen-deuterium exchange to probe conformation and dynamics during various activation states. Proteins that are not amenable to mainstream structural techniques such as X-ray diffraction and NMR can be probed with such methods. Such experiments, among other things, can reveal the effects and locations of binding, be diagnostic for proper protein folding, and be used to determine conformational changes during protein function. He has published over 35 papers on the topic of hydrogen exchange in recent years and given an equal number of invited lectures. He co-organized the 2006 Sanibel conference on studying proteins with hydrogen exchange and now leads an interest group on the topic for the American Society for Mass Spectrometry. Current research projects in his laboratory include (1) investigations of kinase conformation to understand their regulation and aberrant signaling in various disease states including cancer, (2) analysis of the conformation of viral accessory proteins from HIV and several Herpesviruses, and (3) optimization and methods development in hydrogen exchange mass spectrometry.
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