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The impact of membranes on peripheral membrane protein conformation and dynamics can be studied with our new methods using Langmuir monolayers.  See Paper #1 and its sister, Paper #2.

The analytical aspects of HX MS are reviewed in a new article in the Annual Reviews of Analytical Chemistry.  A key attribute, replication, is further discussed in an editorial in Bioanalysis.      more

Unique affinity attachment allows for continuous flow deuterium labeling of captured proteins. read more

In collaboration with Mike Ramsey's group at UNC-Chapel Hill, capillary electrophoresis separations for HX MS were demonstrated.
         Analytical Chemistry article


The laboratory of John R. Engen at Northeastern University performs research at the interface of Analytical Chemistry, Biochemistry & Structural Biology.


We use hydrogen exchange and mass spectrometry (HX MS) as our core technology to probe protein conformation, conformational changes, dynamics, protein folding and the effects of binding.

In the past 14 years, we have applied HX MS to the study of nearly 100 proteins.