LATEST NEWS older news

Lab personnel receive awards:
       Tyler Kolfrat
  Wolfgang Goetzinger–Amgen Memorial
  Undergraduate Scholar Award

HX MS contributes to our understanding of how substrates are recognized and then degraded by the proteasome.
                   Read the paper here 

Not all SH3 domains are the same.  Despite sequence similarity, and tertiary structure homology, the motions these domains undergo in solution can be unique.
A new paper explores Tec family SH3 domains.

A new paper describes the optimal tuning of a StepWave in order to maximum deuterium recovery.


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 15 years, we have applied HX MS to the study of over 100 proteins.