Regensburg 2010 – scientific programme

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SYMR: Symposium Nuclear Magnetic Resonance: from Applications in Condensed-Matter Physics to New Frontiers

SYMR 7: Biopolymers and Biomaterials

SYMR 7.10: Talk

Wednesday, March 24, 2010, 16:45–17:00, H37

Protein folding monitored at six different magnetic field strengths — •Michael Kovermann and Jochen Balbach — Institut für Physik/Fachgruppe Biopyhsik, Martin-Luther-Universität Halle-Wittenberg, Betty-Heimann-Straße 7, D-06120 Halle/Saale, Germany

The folding mechanism of an elongated polypeptide chain into its native three dimensional structure is still of high common interest. Using NMR spectroscopy we are able to follow the permanently occuring folding and unfolding of the cold shock protein B from Bacillus subtilis, BsCspB, in equilibrium and kinetically on a ms timescale.

So-called NMR relaxation dispersion experiments are able to monitor these dynamic events on a ms - to - µs timescale at atomic resolution. We performed these kind of experiments at six different magnetic field strengths to get reliable results. As the folding (and the unfolding) rate of a protein should be independent of the external magnetic field strength we fitted this kinetic parameter in a global procedure to the NMR relaxation data. In addition to these folding rates we get out structural and thermodynamic information by these dynamic NMR experiments.