Abstract
Mass spectrometry can be applied to a variety of analytical problems. One of the less utilized areas of mass spectrometry is the analysis of protein conformation and dynamics. By labeling protein molecules under physiological conditions, either covalently or non-covalently, information can be captured about their folded state. Hydrogen exchange methods non-covalently label the backbone amide hydrogens of proteins with deuterium and the location and magnitude of the labeling can then be determined with mass spectrometry. Details of the methodology will be given and examples of the utility of hydrogen exchange methods will be shown for proteins of importance to the biotechnology and pharmaceutical industries. A more detailed example of the analysis of Src-family kinases relevant to cancer will also be given. In these studies, the role and magnitude of conformational changes upon binding and intramolecular interactions in the Hck and Abl kinases were determined.

Speaker Background John R. Engen is an Associate Professor of Chemistry & Chemical Biology at Northeastern University in Boston. He also holds the position of Faculty Fellow in the Barnett Institute of Chemical and Biological Analysis. Prior to coming to Northeastern, he was an Assistant Professor of Chemistry, Biochemistry and Molecular Biology at the University of New Mexico in Albuquerque and a Member of the University of New Mexico Cancer Center. Professor Engen holds two BS degrees (molecular biology and biochemistry) from Union College and a PhD in Chemistry from the University of Nebraska (working with David L. Smith). He completed postdoctoral work at the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany and at Los Alamos National Laboratory. He is a Fellow of the European Molecular Biology Organization (EMBO).Professor Engen has become a recognized expert in the area of understanding proteins and protein conformation with mass spectrometry. He uses hydrogen-deuterium exchange to probe conformation and dynamics during various activation states. Proteins that are not amenable to mainstream structural techniques such as X-ray diffraction and NMR can be probed with such methods. Such experiments, among other things, can reveal the effects and locations of binding, be diagnostic for proper protein folding, and be used to determine conformational changes during protein function. He has published over 35 papers on the topic of hydrogen exchange in recent years and given an equal number of invited lectures. He co-organized the 2006 Sanibel conference on studying proteins with hydrogen exchange and now leads an interest group on the topic for the American Society for Mass Spectrometry. Current research projects in his laboratory include (1) investigations of kinase conformation to understand their regulation and aberrant signaling in various disease states including cancer, (2) analysis of the conformation of viral accessory proteins from HIV and several Herpesviruses, and (3) optimization and methods development in hydrogen exchange mass spectrometry.

Meeting details

Date:	Thursday	February 21, 2008
Time:	6:00 pm	Social hour, registration (no-host cocktails)
	7:00 pm	Dinner
	8:00 pm	Presentation
Dinner:	featuring:	Crispy-Skin Black Sea Bass with Dill Butter Sauce, Yukon Gold Potatoes, Fennel Puree
		Flank Steak with Anise Marinade
		Mediterranean Farfalle Pasta with Sun Dried Tomatoes, Olives, Basil, Mushrooms & Baby Spinach
		Chicken Piccata sautéed with Lemon, Capers and White Wine
Cost:	$40	BAMS members*
	$50	Non-members
	$60	BAMS membership plus dinner cost
	$20	Students only
	$300	2008 Corporate Sponsors
		Dinner reservations required by noon on Tuesday, February 19, 2008

*Note:  BAMS memberships are for the calendar year and should be renewed with the first event you attend in 2008.  Dues ($30.00) may be paid while registering for dinner.  If you are unsure of your Membership status, please email Tim Hawkins.

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