AT THE INTERFACE OF ANALYTICAL CHEMISTRY, BIOCHEMISTRY & STRUCTURAL BIOLOGY
The laboratory of John R. Engen at Northeastern University uses hydrogen deuterium exchange (HDX) and mass spectrometry (MS) as our core technology to probe protein conformation, conformational changes, dynamics, protein folding and the effects of binding. In the past 22 years, we have applied HDX MS to the study of hundreds of proteins. Learn more
February 2023. In collaboration with Elena Klimtchuk, Lawreen Connors and Olga Gursky at BUSM Amyloidosis Center, we show how the CDRs in IgG light chains contribute to amyloid formation. Read more on bioRxiv.
December 2022. Increase the flow rate for HDX MS – separations will greatly improve. Read more in our article in the Journal of Chromatography A.
September 2022. Our collaboration with David Balchin and F. Ulrich Hartl on protein folding on the ribosome is released on bioRxiv.
July 2022. Our simple, two-part protocol for preparation of a maximally deuterated control sample for HDX MS is published in Analytical Chemistry. Read here.