Hydrogen exchange mass spectrometry to probe the conformation of proteins both in solution and in membranes

John R. Engen

Northeastern University, Boston, MA 02115-5000

j.engen@neu.edu

A continually growing area of mass spectrometry is the analysis of protein conformation and dynamics. One classic approach is to label protein molecules in solution under physiological conditions as the incorporation of the labeling agent is a function of the folded conformation. Hydrogen exchange (HX) methods label the backbone amide hydrogens of proteins with deuterium and the location and magnitude of the labeling can then be determined with mass spectrometry (MS). HX MS studies are particularly well suited for analysis of proteins that will not crystallize, proteins not amenable to NMR, or proteins available in only small quantities. This presentation will explore current methodology and applications of HX MS, both for multi-protein systems in solution and for the analysis of membrane proteins using liposomes or phospholipid nanodiscs.