Prof John R Engen has partnered Waters Corporation to better understand the conformation, or the folded three-dimensionality, of proteins that are thought to play a major role in some diseases.
Alongside Waters Corporation, Prof Engen, an associate professor of chemistry and chemical biology and a faculty fellow at Northeastern University's Barnett Institute of Chemical and Biological Analysis, has pioneered the combined use of hydrogen-deuterium (H/D) exchange technology, Ultraperformance LC and ion mobility mass spectrometry.
By being able to form a better three-dimensional picture of these proteins and how they move and react with other proteins, scientists are able to better understand the relationship between protein function and protein structure and, it is hoped, gain new perspectives on how diseases begin and progress.
Proteins are carefully structured, three-dimensional, long-chain molecules that when properly folded regulate normal bodily functions.
Several high-profile diseases including Alzheimer's, Creuzfeldt-Jakob's and Parkinson's can develop 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 has the ability to monitor individual proteins and protein complexes.
Waters and Prof Engen's laboratory at the Barnett Institute for Chemical and Biological Analysis entered into the scientific collaboration in 2007.
To further Prof Engen's experimental technique, Waters engineers constructed a specially-designed programmable cooling chamber for the Waters Nanoacquity UPLC system, recently described in Analytical Chemistry.
Waters introduced the Synapt High-Definition MS (HDMS) system at the American Society of Mass Spectrometry annual meeting in Seattle in June of 2006.
It is a commercially available mass spectrometer with the ability to analyse ions by their size, shape and charge, in addition to mass.
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.
