Regensburg 2007 – scientific programme
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BP: Fachverband Biologische Physik
BP 26: Poster Session II
BP 26.19: Poster
Thursday, March 29, 2007, 17:00–19:30, Poster B
Interaction potential of Lysozyme and Insulin and denaturation properties of Staphylococcal Nuclease - SAXS studies on aqueous solutions at DELTA synchrotron — •Chris Krywka1, Nadeem Javvid2, Michael Sulc2, Vytautas Smirnovas2, Roland Winter2, and Metin Tolan1 — 1Fachbereich Physik, DELTA, Universität Dortmund, D-44221 Dortmund — 2Fachbereich Physikalische Chemie, Universität Dortmund, D-44227 Dortmund
The influence of various cosolvents on the native state structure of Lysozyme and Insulin in aqueous solution was studied using small-angle x-ray scattering (SAXS) measurements at beamline BL9 of DELTA synchrotron. A wide range of concentrations of both pure protein and with with added cosolvents (tetrafluoroethylene, sodium chloride, ethanol, trimethylaminoxyd, glycerol) was probed. For the higher concentrated samples information about the intermolecular interaction potential could be obtained from analysis of the structure factor. Unlike Lysozyme and Insulin, Staphylococcal Nuclease can fold and unfold reversibly due to the lack of disulfide bonds or free sulfhydryl groups. This allows to study the intermediate states of unfolding and refolding induced by temperature or pressure, close to the native and denaturated state. SAXS measurements were performed in a wide pressure and temperature range (1 bar to 6 kbar and -10°C to 65°C) in the absence and presence of various cosolvents (tetrafluoroethylene, glycerol, urea, sodium chloride) and the changes in tertiary structure of the different conformational states were analysed.