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In collaboration with the Walensky lab at HMS/DFCI, the interactions between the apoptosis protein Bax and a stapled peptide from Bcl-2 were studied. The stapled peptide prevents conformational activation of Bax, keeping cells alive.     Paper in Molecular Cell

Lab personnel receive awards:
   Kristian Teichert
       Provost Undergraduate Creative
       Endeavors Award

A new survey of the applications of hydrogen / deuterium exchange mass spectrometry from 2012-2014 shows its widespread appeal.

Read the article in Analytical Chemistry issue "Fundamental and Applied Reviews in Analytical Chemistry 2015"


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 13 years, we have applied HX MS to the study of more than 75 proteins.