Dresden 2006 – wissenschaftliches Programm
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AKB: Biologische Physik
AKB 40: Poster Session II
AKB 40.33: Poster
Mittwoch, 29. März 2006, 16:30–19:30, P3
Dynamics of the denaturated protein Ribonuclease A — •Ralf Biehl1, Bernd Hoffmann2, Michael Monkenbusch1, Aurel Radulescu1, Bela Farago3, Rudolf Merkel2, and Dieter Richter1 — 1Institut fuer Festkoerperforschung, Forschungszentrum Juelich, Germany — 2Institut fuer Schichten und Grenzflaechen, Forschungszentrum Juelich, Germany — 3Institut Laue-Langevin, Grenoble, France
The protein folding and function is strongly coupled to the structure and the thermal equilibrium fluctuations. In view of the macromolecule energy landscape the protein folding follows a path from the unfolded state at high energy to the low energy state at the final configuration with intermediate states in between. Thereby the secondary and ternary structure is determined. Catalytic activities or transport mechanisms follow transitions between intermediate states in the energy landscape. All involve configurational changes on length scales from single amino acids to sizes of complete a helices or b sheets and the total size of the protein. Timescales reach from picoseconds to microseconds. A way to explore the energy landscape at equilibrium is to observe thermal fluctuations of the protein. By changing environmental parameters e.g. temperature the level of energy is changed. We present here measurements on bovine Ribonuclease A by means of SANS and Neutron Spinecho Spectroscopy together with DLS measurements. The protein dynamics was examined under conditions providing the possibility of refolding to the natural state. We compare our experimental results with simple and more complex protein models to reproduce the observed dynamics.