Collisions, photons, electrons and protein complexes: Gas-phase structural analysis with FTICR-MS

ANYL 326

Ron MA. Heeren, heeren@amolf.nl1, Rimco B. J. Geels1, Saskia M. van der Vies2, and Albert J R Heck, a.j.r.heck@chem.uu.nl3. (1) FOM-Institue for Atomic and Molecular Physics, Kruislaan 407, 1098 SJ, Amsterdam, Netherlands, (2) Department of Biochemistry and Molecular Biology, Vrije Universiteit Amsterdam, De Boelelaan 1083, Amsterdam, 1081 HV, Netherlands, (3) Utrecht University, Department of Biomolecular Mass Spectrometry, Sorbonnelaan 16, Utrecht, 3584 CA, Netherlands
Using electrospray ionization, non-covalently bound protein complexes can be transferred intact into the gas-phase and analyzed and manipulated in a mass spectrometer. Modern mass spectrometric techniques can be used to determine complex stochiometry as well as protein composition and sequence. The activation of these macromolecular complexes is far from trivial. The large number of degrees of freedom combined with various hydrogen bonds hamper extensive fragmentation using conventional activation techniques. Low resolution mass spectrometric techniques often used to study these systems such as modified q-ToF mass spectrometers allow little or no dissociation techniques other than collisional activation to be applied. Fourier Transform Ion Cyclotron Resonance Mass Spectrometry (FTICR-MS) has the unique capabilties to employ different internal energy deposition methods to structurally study these large non-covalently bound protein complexes. In this contribution we will employ collisions, infrared multiphoton dissociation and electron capture dissociation to study the gas-phase fragmentation behavior of large multimeric protein complexes.
 

Frank H. Field and Joe L. Franklin Award for Outstanding Achievement in Mass Spectrometry in Honor of Jean H. Futrell
8:30 AM-12:20 PM, Tuesday, August 21, 2007 BCEC -- 104B, Oral

Division of Analytical Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007