Lars Konermann Professor Ph.D. (Max Planck Institute, Univ. of Düsseldorf, Germany) Office and Lab: BGS 2016 Phone (Office): (519) 661-2111 ext. 86313 Phone (Lab): (519) 661-2111 ext. 86667
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Protein Mass Spectrometry. Biophysical and Bioanalytical Chemistry
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Awards:
• Canada Research Chair
• Premier's Research Excellence Award
• Fred Beamish Award of the Canadian Society for Chemistry
• USC Teaching Honour Roll Award of Excellence
• Faculty of Science Award of Excellence in Undergraduate Teaching (2004)
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Current Research Programs:
Our group is interested in exploring the folding mechanisms of proteins, their conformational dynamics, and their interactions with other molecules. We specialize in the development and application of novel electrospray mass spectrometry (ESI-MS) techniques for this purpose. This research bridges the areas of biophysics, biochemistry, and analytical chemistry.
The question how and why a highly disordered protein chain can spontaneously refold into its native structure remains one of the major unsolved problems in biophysical chemistry. Research in this area is of fundamental importance for understanding the factors responsible for protein folding-related diseases such as Alzheimer's and BSE.
Mass spectrometry in conjunction with rapid mixing techniques allows the detection and characterization of short-lived intermediates, thereby providing important insights into the mechanisms by which proteins fold and assemble into quaternary structures. The information from these experiments is complementary to that obtained by optical and NMR spectroscopy.
Other research directions pursued in our laboratory include studies on protein-ligand binding and enzymatic reaction mechanisms.
Selected Publications:
"Folding Kinetics of the S100A11 Protein Dimer Studied by Time-Resolved Electrospray Mass Spectrometry and Pulsed Hydrogen/Deuterium Exchange" J. Pan, A. C. Dempsey, Y. Li, G. S. Shaw, and L. Konermann Biochemistry 45, 3005-3013 (2006).
"Pulsed Hydrogen Exchange and Electrospray Charge-State Distribution as Complementary Probes of Protein Structure in Kinetic Experiments: Implications for Ubiquitin Folding" J. Pan, D. J. Wilson, and L. Konermann Biochemistry 44, 8627-8633 (2005).
"Subunit Disassembly and Unfolding Kinetics of Hemoglobin Studied by Time-Resolved Electrospray Mass Spectrometry" D. A. Simmons, D. J. Wilson, G. A. Lajoie, A. Doherty-Kirby, and L. Konermann, Biochemistry 43, 14792-14801 (2004).
"A Capillary Mixer With Adjustable Reaction Chamber Volume for Millisecond Time-Resolved Studies by Electrospray Mass Spectrometry" D. J. Wilson and L. Konermann, Anal. Chem. 75, 6408-6414 (2003).
"Characterization of Transient Protein Folding Intermediates During Myoglobin Reconstitution by Time-Resolved Electrospray Mass Spectrometry with On-Line Isotopic Pulse Labeling" D. A. Simmons and L. Konermann Biochemistry 41, 1906-1914 (2002).
