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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