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LATEST NEWS older news

We review HX MS of chaperones in protein folding.  Goes well with previous papers on protein complexes and signaling complexes.
 

Fgr: The Src-family maverick
Although its 3-D arrangement may be similar to other Src-family kinases, Fgr kinase regulation seems to be atypical.     Read more here.  

We describe how mutations in the main protein of HDL, apolipoprotein A-I, affect protein conformation.  This study is part of a collaboration with the laboratory of  Olga Gursky at BUMC.   Read article here

Isaac Kresse awarded a Barry Goldwater Scholarship.  Read more about Isaac and the other Northeastern University winners.

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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 20 years, we have applied HX MS to the study of hundreds of proteins