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BP: Fachverband Biologische Physik
BP 7: Posters: Proteins
BP 7.19: Poster
Montag, 26. März 2012, 17:30–19:30, Poster A
Ribonuclease A: A Model System to Study Structure and Dynamics of Disordered Proteins — •Jennifer Fischer1, Ralf Biehl1, Bernd Hoffmann2, and Dieter Richter1 — 1Forschungszentrum Jülich, ICS-1, Jülich, Germany — 2Forschungszentrum Jülich, ICS-7, Jülich, Germany
Up to know structure and dynamics are believed to play the key role in protein function. Now it is evident that roughly 30% of eukaryotic proteins are partially or even completely unfolded [1]. Nevertheless, intrinsically unfolded proteins are functional and involved in several biological processes. To get further insight into disordered structures and their dynamics, we use Ribonuclease A (RNase A) as a model system, as it is a well known protein denaturing reversibly upon heating. Additionally, by varying the buffer conditions such as pH values and by reducing the disulfide bonds, several states can be prepared. A detailed study of the structure and dynamics using Small Angle Neutron and X-ray Scattering (SANS, SAXS) as well as Neutron Spin Echo Spechtroscopy (NSE) and Circular Dichroism Spectroscopy is presented. The combination of these techniques allows us to observe large-scale internal dynamics of subdomains or of unfolded protein strands that operate on the same length scale as rotational diffusion. However, the timescale can be different and depends on the protein structure and internal interactions. [1] A. L. Fink, Current Opinion in Structural Biology 2005, 15:35-41