and Mass Spectrometry

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FT-ICR Mass Spectrometry: Infrared Multiphoton Dissociation as Probes of Protein Structure and Non-Covalent Binding in Solution and Gas Phase

presented by

Alan Marshall
Florida State University

March 17, 1999

The Scripps Research Institute, W.M. Keck Foundation Amphitheater


Dr. Marshall has earned numerous honors and awards throughout his career, including the American Chemical Society Award in Chemical Instrumentation in 1990 and the American Chemical Society Field-Franklin Award in Mass Spectrometry for 1995. In addition to contributing to 277 publications, 3 U.S. patents and several books, as well as serving on numerous editorial boards and fulfilling the role of North American Editor of Rapid Communications in Mass Spectrometry.


Mass spectrometry is complementary to NMR in analyzing H/D exchange as a probe of protein surface accessibility in solution: NMR probes every amide backbone proton, but MS can resolve multiple conformations, as well as extend measurements to proteins too large, too insoluble, or bound to other proteins. In particular, MS can map contact surfaces between two non-covalently bound proteins. In the gas phase, FT-ICR MS can sort (by gaseous H/D exchange) and isolate different protein conformations, and can determine the activation energy to break non-covalent complexes. Comparison of solution- and gas-phase behavior offers direct evidence for the effect of water on protein structure and binding.

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