Campus Event Calendar
Event Entry
What and Who
Protein Folding and Conformational Dynamics: What Can Mass Spectrometry Experiments Tell Us?
Lars Konermann
University of Western Ontario
Talk
AG 1, AG 2, AG 3, AG 4
MPI Audience
Note: We use this to send email in the morning.
Date, Time and Location
Tuesday, 8 July 2003
16:00
-- Not specified --
046
021
Saarbrücken
Abstract
The 2002 Nobel Prize in Chemistry has highlighted the tremendous importance of
mass spectrometry (MS) for modern biology. Our laboratory is specialized on the
use of MS for studying protein folding. We have developed methods capable of
tracking the conformational changes of polypeptide chains as a function of
time, as well as interactions of proteins with noncovalent binding partners.
These experiments are based on the combination of MS with rapid mixing methods
and on-line isotope exchange; they can provide a detailed understanding of
protein folding mechanisms, and on the multidimensional energy landscapes of
polypeptide chains. Similar methods can be applied to monitor the
conformational dynamics ("breathing motions") of proteins under equilibrium
conditions. Other topics of interest include mechanistic studies on
enzyme-catalyzed processes, as well as novel screening methods that hold great
promise for the identification of specific drug-protein interactions.
Some key references:
"Protein Folding Kinetics and Mechanisms Studied by Pulse-Labeling and Mass
Spectrometry" L. Konermann and D. A. Simmons, Mass Spectrom. Rev. 22, 1-26
(2003).
"Conformational Dynamics of Partially Denatured Myoglobin Studied by
Time-Resolved Electrospray Mass Spectrometry With Online Hydrogen- Deuterium
Exchange" D. A. Simmons, S. D. Dunn and L. Konermann, Biochemistry 42,
5896-5905 (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).
mass spectrometry (MS) for modern biology. Our laboratory is specialized on the
use of MS for studying protein folding. We have developed methods capable of
tracking the conformational changes of polypeptide chains as a function of
time, as well as interactions of proteins with noncovalent binding partners.
These experiments are based on the combination of MS with rapid mixing methods
and on-line isotope exchange; they can provide a detailed understanding of
protein folding mechanisms, and on the multidimensional energy landscapes of
polypeptide chains. Similar methods can be applied to monitor the
conformational dynamics ("breathing motions") of proteins under equilibrium
conditions. Other topics of interest include mechanistic studies on
enzyme-catalyzed processes, as well as novel screening methods that hold great
promise for the identification of specific drug-protein interactions.
Some key references:
"Protein Folding Kinetics and Mechanisms Studied by Pulse-Labeling and Mass
Spectrometry" L. Konermann and D. A. Simmons, Mass Spectrom. Rev. 22, 1-26
(2003).
"Conformational Dynamics of Partially Denatured Myoglobin Studied by
Time-Resolved Electrospray Mass Spectrometry With Online Hydrogen- Deuterium
Exchange" D. A. Simmons, S. D. Dunn and L. Konermann, Biochemistry 42,
5896-5905 (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).
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