Exploring the conformational diversity of proteins and peptides using high-resolution FAIMS and IMS

ANYL 227

Keqi Tang, keqi.Tang@pnl.gov1, Alexandre A. Shvartsburg1, Fumin Li1, Yehia Ibrahim1, David C. Prior2, Michael A. Buschbach2, Erin S. Baker1, and Richard D. Smith, rds@pnl.gov3. (1) Biological Sciences Division, Pacific Northwest National Laboratory, Battelle Boulevard, PO Box 999, Richand, WA 99352, (2) Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Battelle Boulevard, PO Box 999, Richand, WA 99352, (3) Pacific Northwest National Laboratory, P.O. Box 999 (K8-98), 3335 Q. Ave., Richland, WA 99352
Understanding the 3-D structure and dynamics of proteins and other biological macromolecules in various environments is among the central challenges of modern biology. Both conventional ion mobility spectrometry (IMS) and field asymmetric waveform IMS (FAIMS) can separate isomeric mixtures with high sensitivity and speed. However, the separation peak capacity of either FAIMS or IMS alone is generally insufficient for the conformational diversity of protein and peptide ions. Here we investigate protein and peptide conformations by 2-D FAIMS/IMS (coupled to mass spectrometry), with high FAIMS resolution provided by a new planar geometry analyzer. Effective ion transmission between stages is achieved by employing novel slit-aperture and electrodynamic ion funnel interfaces, including a new higher pressure ion funnel design. Isomerization pathways of specific precursors are probed using collisional activation of ions between FAIMS and IMS stages, in analogy to the MS/MS approach for studying fragmentation pathways.
 

Bioanalytical Applications of Ion Mobility Mass Spectrometry, Supported by Waters Corporation
8:30 AM-12:05 PM, Tuesday, 12 September 2006 Moscone Center -- Room 124, Oral

Division of Analytical Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006