February 2009 Meeting Announcement, Delaware Valley Mass Spectrometry Discussion Group
- Topic: "Proteomics-Mass Spectrometry: Combining Electrophoresis with Mass Spectrometry to Maximize Proteome Information
- Speaker: David H. Russell (Texas A&M University)
- Date: Monday, February 9, 2009. 6:30 PM
- Time: Social Hour: 6:30 PM.
Talk: 7:30 PM.
Please RSVP to John Masucci JMASUCCI@PRDUS.JNJ.COM by Thursday February 5th.
- Place: Department of Chemistry, Villanova University (Room 154, Mendel Hall)
A goal of our research is to develop multi-dimensional separations techniques that will allow us to increase chemical information content using mass spectrometry based proteomics. For example, we have combined off-line capillary electrophoresis (CE) with matrix assisted laser desorption/ionization (MALDI) - mass spectrometry (MS) to facilitate peptide identification and compositional information, viz. determining the number of basic amino acid residues in a peptide.1 We also developed a novel isoelectric point (pI) based separation device termed membrane separated wells for isoelectric focusing and trapping (MSWIFT) which allows for quick in-solution separations of ampholytes.2 In addition, we have used MSWIFT in combination with CE-MALDI-MS for rapid analysis of protein mixtures and mixtures of protein proteolytic digests. Lastly, we have combined CE-MALDI-MS and MSWIFT-CE-MALDI-MS with ion mobility-mass spectrometry (IM-MS) to enhance protein ID, determination of post-translational modification, and information content for applications of imaging mass spectrometry of lipid bilayers. This presentation will focus on analytical figures-of-merit for extensive hyphenation of analytical methodologies as well as presentation of results that underscore the utility of these experimental approaches.
(1) Williams, B. J.; Russell, W. K.; Russell, D. H. Analytical Chemistry 2007, 79, 3850-3855.
(2) Lim, P.; North, R.; Vigh, G. Electrophoresis 2007, 28, 1851-1859.
David H. Russell, MDS-Sciex Professor of Mass Spectrometry, Director, Laboratory for Biological Mass Spectrometry (LBMS), and Assoc. Director Center for Structural Biology directs an internationally recognized research program in developmental mass spectrometry. The LBMS is unique among mass spectrometry facilities because the research programs include development of new instrument technologies, fundamental research on the chemistry of gas-phase ions, esp. peptides and proteins, and applications of mass spectrometry to basic chemistry, bio-analytical chemistry, and modern chemical-biology. The LBMS was the pilot program (est. 1994) for the TAMU Research Infrastructure Program. The research in the LBMS ranges from development of new instrumentation and laser techniques for molecular imaging using matrix-assisted laser desorption ionization (MALDI) and ion mobility-mass spectrometry, and the capabilities of this new technology far exceeds that of similar research at other institutions. In addition, the LBMS is currently involved in collaborative research (instrument/technique development) with mass spectrometry companies as well as biological (primarily proteomics) researchers at TAMU and other academic/industrial laboratories.
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