John Engen
Northeastern University
John R. Engen is the James L. Waters Chair in Analytical Chemistry and a COS Distinguished Professor of Chemistry & Chemical Biology at Northeastern University in Boston. Professor Engen earned two B.S. degrees (one in molecular biology and one in 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 the Los Alamos National Laboratory. In 2002 he became an Assistant Professor of Chemistry, Biochemistry and Molecular Biology at the University of New Mexico in Albuquerque and moved to Northeastern University in 2006. In 2012-2013, he was a Visiting Professor of Biochemistry in the laboratory of Prof. F. Ulrich Hartl at the Max Planck Institute of Biochemistry in Martinsried, Germany; in 2019-2020 he was a Visiting Professor of Cell Biology in the laboratory of Tom Rapoport at Harvard Medical School. At Northeastern University, he has received both the Excellence in Teaching Award (2015) and the Excellence in Research and Creative Activity Award (2021), the highest awards in teaching and research given by the University. In 2019 he was named the James L. Waters Chair in Analytical Chemistry.
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 HX MS. Such experiments, among other things, can reveal the effects and locations of protein:ligand binding, be diagnostic for proper protein folding, and be used to determine conformational changes during protein function.
Professor Engen has published over 175 papers on the topic of hydrogen exchange in recent years and given hundreds of invited lectures to academia and industry. He teaches a yearly ASMS short course on protein structural analysis by mass spectrometry. Current research projects in his laboratory include studies of proteins related to apoptosis, kinases, large proteins and protein complexes, protein folding machinery, and improving the analytical aspects of HX MS technology including resolving power & commercial availability.
More information available at https://neu.hxms.com
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 HX MS. Such experiments, among other things, can reveal the effects and locations of protein:ligand binding, be diagnostic for proper protein folding, and be used to determine conformational changes during protein function.
Professor Engen has published over 175 papers on the topic of hydrogen exchange in recent years and given hundreds of invited lectures to academia and industry. He teaches a yearly ASMS short course on protein structural analysis by mass spectrometry. Current research projects in his laboratory include studies of proteins related to apoptosis, kinases, large proteins and protein complexes, protein folding machinery, and improving the analytical aspects of HX MS technology including resolving power & commercial availability.
More information available at https://neu.hxms.com