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BP: Fachverband Biologische Physik

BP 7: Poster I

BP 7.27: Poster

Monday, March 23, 2009, 17:45–20:00, P3

Probing the unfolding behavior of SNase mutants by SAXS — •Martin Schroer¹, Christina Krywka², Saskia Schmacke¹, Michael Paulus¹, Roland Winter³, Catherine Royer⁴, Bertrand Garcia-Moreno⁵, and Metin Tolan¹ — ¹Fakultät Physik/DELTA, Technische Universität Dortmund, D-44221 Dortmund, Germany — ²Institut für Experimentelle und Angewandte Physik, Christian-Albrechts-Universität zu Kiel, 24118 Kiel, Germany — ³Physikalische Chemie I, Technische Universität Dortmund, D-44227 Dortmund, Germany — ⁴3 CNRS, UMR5048, Centre de Biochimie Structurale, F-34090 Montpellier, France — ⁵Department of Biophysics, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA

Investigating the structure of proteins and their stability is of great interest as it is known that destabilization may lead to protein unfolding, misfolding and aggregation. These effects might be first steps for several diseases such as the Alzheimer disease and prion diseases. In order to get a deeper insight into this process it is thus necessary to determine how the stability and conformation are changed when the protein’s amino acid sequence is altered by point mutations.

In our recent SAXS (small angle x-ray scattering) studies we analyzed the unfolding behavior of different mutants of the model protein Staphylococcal Nuclease (SNase) as a function of temperature and pressure. Depending on the physicochemical properties of the particular amino acid exchanged, the stability of the mutants is altered significantly.