Protein aggregation under Constrainment
The proposal involves the study of protein aggregation under volume constraints. Lysozyme as a test protein will dissolved in aqueous conditions within the open cages of a lipid cubic phase of monoolein, and the aggregation state will be studied as a function of temperature for three different types of solution conditions: pure water, and solutions of Na2SO4 or NaJ as examples for kosmotropic resp. chaotropic salt solutions. The two different hydration conditions within the salt solutions will modulate the details of the cubic phase by widening / narrowing its pore radii, thus as well modifying the aggregation conditions of the dissolved macromolecule. Contrast matching methods will give access to clearly distinguishing scattering contributions due to the structure of the cubic phase from the SANS signal of the dissolved macromolecules, allowing to extract the details of the composite system in separate subsequent experiments. D11, with its high flux, is a perfect choice for that kind of experiment.
Please note that you will need to login with your ILL credentials to download the data.
Download DataThe recommended format for citing this dataset in a research publication is in the following format:
Beate Klösgen; CHRISTENSEN Christian Kolle; LINDNER Peter and TANAKA Shinpei. (2013). Protein aggregation under Constrainment. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-520
ILL has partnered with DataCite as the registration agency
for data persistent identifiers.