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Work recently published in the journal Structure shows that although tertiary structure may be known from crystal structure determination, protein dynamics can not be easily predicted.  Proteins with highly similar shape may move and flex differently in solution and this could have an impact on function.      More details

Feb 2014 cover story in BioPharm International on higher order structure determination for protein therapeutics, including comments from Prof. Engen on the use of HDX-MS.    Read article      NEU 3Q's
   BioPharm International website         Lexicon

Hydrogen exchange MS shows how peptide binding affects a transmembrane 95 kDa glycosylated protein embedded in a phospolipid nanodisc.  Such studies will make conformational analyses of many membrane proteins and protein complexes feasible.          More details


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 10 years, we have applied HX MS to the study of more than 60 proteins.