Konermann honoured for visualizing how proteins fold

By Mitchell Zimmer
July 04, 2013

LarsPhoto by Mitchell Zimmer


While mass spectrometry has been used to analyze amino acids and proteins since 1958, it wasn’t until recently that Lars Konermann found a way to see how proteins change through time into their active conformations. That discovery has earned the Western Chemistry professor two recent honours.

Recently, Konermann received both the Ken Standing Award from Enabling Technologies Symposium (ETP) Inc., recognizing significant contributions to life science technology development, and the Fred P. Lossing Award from the Canadian Society for Mass Spectrometry, highlighting a distinguished Canadian mass spectrometrist.

“In my case, we did some work to figure out how we can monitor how proteins fold,” Konermann said. “This is a very important biological process. So, this is something that we worked on a lot. We also applied some of the methods that we developed to look at proteins in aggregates that are implicated in Alzheimer’s disease.”

One of the other problems Konermann pursues is how proteins with many individual subunits, such as microtubules and flagella, come together.

“We can see how this works and what the intermediates are along the way,” he said.

Protein systems like these spontaneously self assemble, and Konermann monitors these processes by analyzing samples taken at many different time points, ranging from milliseconds to hours. He then sprays each sample into the mass spectrometer.

“In the simplest case, just by doing a mass measurement, we can see how many things are assembled,” he said.  “You can see when the mass has doubled; the next thing we have four mass units and so now it’s four, it goes from there.”

The most recent work in Konermann’s lab involves monitoring how proteins fold. He has developed techniques allowing him to monitor these conformational changes almost at the atomic level by using hydrogen-deuterium exchange or covalent labeling techniques.

Konermann, Canada Research Chair of Biophysical Protein Mass Spectrometry, completed his PhD in the area of plant photosynthesis in 1996 at the Max Planck Institute in Mulheim (Germany), supervised by A. R. Holzwarth. He was first exposed to the world of biological mass spectrometry while working as post-doctoral fellow from 1996 -98 with D. J. Douglas at the University of British Columbia in Vancouver.

He has received the CSC Fred Beamish Award in 2003, UWO Florence Bucke Award in 2011 and several teaching awards. He was a member of the NSERC Chemistry Evaluation group (2009-11), chaired the 2011 Gordon Conference on Biological Molecules in the Gas Phase and in Solution, and he is a current member of the editorial board for the Journal of The American Society for Mass Spectrometry.


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