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American Chemical Society Awards John R. Engen for Scientific Achievements
Date:9/1/2009

velop when certain proteins become misfolded, causing a chain of events that can lead to disease symptoms. Thus understanding how a protein achieves its folded state is important. Mass spectrometry is unique in its ability to monitor individual proteins and protein complexes.

Prof. Engen has published extensively on the H/D technique, most recently in the Proceedings of the National Academy of Sciences, and in a feature article for Analytical Chemistry. Waters and Prof. Engen's laboratory at the Barnett Institute for Chemical and Biological Analysis entered into a scientific collaboration in 2007. To further Prof. Engen's experimental technique, Waters engineers constructed a specially-designed programmable cooling chamber for the Waters(R) nanoACQUITY(R) UPLC System, recently described in Analytical Chemistry.

Waters introduced the SYNAPT(TM) High Definition MS (TM) (HDMS(TM)) System at the American Society of Mass Spectrometry annual meeting in Seattle in June of 2006. It is the first commercially-available mass spectrometer with the ability to analyze ions by their size, shape and charge in addition to mass.

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