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Electrospray Mass Spectrometry: Fundamentals and Practicalities for Protein Analyses

presented by

Richard B. Cole
University of New Orleans

March 25, 2005

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


Background:

Present Titles:


  • University Research Professor of Chemistry

  • Director, Center for Mass Spectrometry Research


Area of Specialization:

  • Analytical / Bio-organic Mass Spectrometry



Education:

  • Post-Doctoral Research Associate, Universit? Paris (VI) and Ecole Polytechnique, France, 9/86-9/87

  • Ph.D., University of North Carolina at Chapel Hill, 8/86 (Analytical Chemistry)

  • M.S., University of Illinois at Champaign/Urbana, 8/82 (Analytical Chemistry)

  • B.A., Grinnell College, Grinnell, IA, 5/78 Chemistry

  • B.A., Grinnell College, Grinnell, IA, 5/78 French
  • Abstract:

    The talk will be divided into three parts starting with an overview of fundamental aspects of the ionization mechanism in electrospray mass spectrometry with an emphasis on the implications for protein analyses. In the second part, a detailed comparison of charge state distributions obtained for nanospray capillaries of varying diameters will be described. Our findings indicate that the use of narrow diameter capillaries can promote the formation of higher charge state ions that are more reactive precursors in tandem mass spectrometry experiments, or more efficient capturers of electrons in ECD experiments. While mass spectrometry is not traditionally known as a probe for hydrophobically driven noncovalent associations, in the third portion of the talk, detailed electrospray mass spectrometry studies of binding specificities of model fusion peptides with cell membrane phospholipids, i.e, phosphatidylcholines and phosphatidylglycerols will be presented. Viral infections are propagated by the fusing of the viral membrane with a host cell membrane. Fusion peptides must insert into the lipid-rich host cell membrane to initiate rupture and merging of the two entities, but much remains unknown about the details of the fusion process. Results indicate that hydrophobic interactions play a key role in the mass spectrometrically observed binding between fusion peptides and phospholipids. These experiments offer evidence of the ability of ES-MS to provide binding information concerning noncovalent interactions that were established principally by the hydrophobic effect in solution.

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