Office & Lab: Rm 2016 BGS
Phone (Office): ext 86313
Phone (Lab): ext 86667
E-mail: firstname.lastname@example.orgResearch Group
Protein Mass Spectrometry. Biophysical and Bioanalytical Chemistry
Traditional Research Division:
Physical & Analytical
Ph.D. (Max Planck Institute, Univ. of Düsseldorf, Germany)
- Edward G. Pleva Award for Excellence in Teaching (2015)
- Outstanding Reviewer Award, J. Am. Soc. Mass Spectrom. (2015)
- W.A.E. McBryde Medal (2014)
- Fred Lossing Award (2013)
- Ken Standing Award (2013)
- USC Award of Excellence in Undergraduate Teaching (2012)
- Florence Bucke Science Prize (2011)
- Faculty of Science Award of Excellence in Undergraduate Teaching (2005)
- USC Teaching Honour Roll Award of Excellence
- Canada Research Chair (Tier 2, 2004-2014)
- Fred Beamish Award (2003)
- Premier’s Research Excellence Award (2000)
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.
My Research Group Homepage
- 1024a - Chemistry for Engineers
- 2374a - Thermodynamics
- 4490e - Research Project
- 4491e - Chemical Research Discovery and Scientific Communication
- 4494b - Biophysical Chemistry
- 9494b - Biophysical Chemistry
- 9504b - Protein Folding
- "Submillisecond Protein Folding Events Monitored by Rapid Mixing and Mass Spectrometry-Based Oxidative Labeling" S. Vahidi, B. B. Stocks, Y. Liaghati-Mobarhan, and L. Konermann Anal. Chem. 85, 8618–8625 (2013).
- "Activation of ClpP Protease by ADEP Antibiotics: Insights from Hydrogen Exchange
Mass Spectrometry" M. Sowole, J. Alexopoulos, Y.-Q. Cheng, J. Ortega, and L.
Konermann J. Mol. Biol. 425 4508-4519 (2013).
- "Early Hydrophobic Collapse of a1-Antitrypsin Facilitates Formation of a Metastable State: Insights from Oxidative Labeling and Mass Spectrometry" B. B. Stocks, A. Sarkar, P. L. Wintrode, and L. Konermann J. Mol. Biol. 423, 789-799 (2012).
- "Structure and Dynamics of Small Soluble Abeta(1-40) Oligomers Studied by Top-Down Hydrogen Exchange Mass Spectrometry" J. Pan, J. Han, C. H. Borchers, and L.Konermann Biochemistry 51, 3694–3703 (2012).
- "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 J. Am. Chem. Soc. 133, 20237–20244 (2011).