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 earned two B.S. degrees (molecular biology and biochemistry) from Union College and a Ph.D. 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) and was recently recognized with the 2009 Arthur F. Findeis Award from the American Chemical Society.

Professor Engen has become a recognized expert in the area of understanding proteins and protein conformation with mass spectrometry (MS).  He uses hydrogen-deuterium exchange (HX) to probe conformation and dynamics during various activation states.  Proteins that are not amenable to mainstream structural techniques such as X-ray crystallography 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.
 
Professor Engen has published over 40 papers on the topic of hydrogen exchange in recent years and given more than 70 invited lectures to academia and industry.  He led an interest group on HX MS in the American Society for Mass Spectrometry from 2006-2009 and now sits on the Board of Directors for the Society.  Current research projects in his laboratory include (1) investigations of kinase conformation to understand 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.