A Journey Through Protein Mass Spectrometry: From Computer Simulations of the Electrospray Process to Functional Studies on Molecular Motors
Event details
| Date | 07.04.2016 |
| Hour | 16:30 › 17:30 |
| Speaker |
Prof. Lars Konermann Protein Mass Spectrometry Laboratory, Department of Chemistry / Department of Biochemistry, The University of Western Ontario, London, Canada |
| Location | |
| Category | Conferences - Seminars |
Electrospray ionization (ESI) allows the production of desolvated ions from proteins and protein complexes in solution. Analysis of these gaseous biomolecules by mass spectrometry reveals the nature of protein interaction partners. Ion mobility spectrometry and various dissociation experiments provide additional insights. This presentation will focus on two research directions that are being pursued in the Konermann laboratory. At the very “fundamental” end of the spectrum, we conduct experiments and molecular dynamics simulations to uncover the ESI mechanism, and for understanding how proteins respond to the transition from solution into the gas phase. Our work also has a more “applied” side, where hydrogen/deuterium exchange techniques are being used to decipher the inner workings of proteins in solution. As an example, we will highlight recent experiments on ATP synthase, the world’s smallest rotational motor.
Selected Publications:
"Load-dependent destabilization of the γ-rotor shaft in FOF1 ATP synthase revealed by H/D-exchange mass spectrometry" S. Vahidi, Y. Bi, S. D. Dunn, and L. Konermann PNAS in press (2016).
"Release of Native-Like Gaseous Proteins from Electrospray Droplets via The Charged Residue Mechanism: Insights from Molecular Dynamics Simulations" R. G. McAllister, H. Metwally, Y. Sun, and L. Konermann JACS 137, 12667 (2015).
"Molecular Dynamics Simulations of the Electrospray Process: Formation of NaCl Clusters via the Charged Residue Mechanism" L. Konermann, R. G. McAllister, H. Metwally J. Phys. Chem. B 118, 12025 (2014).
"Effects of Protein-Ligand Interactions on Hydrogen/Deuterium Exchange Kinetics: Canonical and Non-Canonical Scenarios" M. A. Sowole and L. Konermann Anal. Chem. 86, 6715 (2014).
"Hydrogen Exchange Mass Spectrometry of Bacteriorhodopsin Reveals Light-Induced Changes in the Structural Dynamics of a Biomolecular Machine" Y. Pan, L. Brown, and L. Konermann JACS 133, 20237 (2011).
"H/D Exchange Mass Spectrometry with Top-Down Electron Capture Dissociation for Characterizing Structural Transitions of a 17 kDa Protein" J. Pan, J. Han, C. H. Borchers, and L. Konermann JACS 131, 12801 (2009).
Selected Publications:
"Load-dependent destabilization of the γ-rotor shaft in FOF1 ATP synthase revealed by H/D-exchange mass spectrometry" S. Vahidi, Y. Bi, S. D. Dunn, and L. Konermann PNAS in press (2016).
"Release of Native-Like Gaseous Proteins from Electrospray Droplets via The Charged Residue Mechanism: Insights from Molecular Dynamics Simulations" R. G. McAllister, H. Metwally, Y. Sun, and L. Konermann JACS 137, 12667 (2015).
"Molecular Dynamics Simulations of the Electrospray Process: Formation of NaCl Clusters via the Charged Residue Mechanism" L. Konermann, R. G. McAllister, H. Metwally J. Phys. Chem. B 118, 12025 (2014).
"Effects of Protein-Ligand Interactions on Hydrogen/Deuterium Exchange Kinetics: Canonical and Non-Canonical Scenarios" M. A. Sowole and L. Konermann Anal. Chem. 86, 6715 (2014).
"Hydrogen Exchange Mass Spectrometry of Bacteriorhodopsin Reveals Light-Induced Changes in the Structural Dynamics of a Biomolecular Machine" Y. Pan, L. Brown, and L. Konermann JACS 133, 20237 (2011).
"H/D Exchange Mass Spectrometry with Top-Down Electron Capture Dissociation for Characterizing Structural Transitions of a 17 kDa Protein" J. Pan, J. Han, C. H. Borchers, and L. Konermann JACS 131, 12801 (2009).
Practical information
- General public
- Free
Organizer
- Prof. Ulrich Lorenz
Contact
- Prof. Ulrich Lorenz