Monitoring the short-time diffusion upon approaching the arrested state
Dissolved proteins can feature rich phase diagrams in the presence of additives. The addition of PEG to antibody solutions lead to liquid-liquid phase separations due to depletion interactions. This LLPS is characterized by a lower critical solution temperature. If the phase boundary is passed fast enough by quenching the temperature, the system can be driven into an arrested state. We use this model system of antibodies and PEG which we have characterized previously with static methods such as SANS and kinetic methods as XPCS. Previous measured elastic fixed window scans on neutron back scattering instruments showed time dependent changes in the scattering signal after the quench. To be able to separate the global and internal dynamics of the proteins, we aim for measuring full QENS spectra using a floating average to capture time dependent changes next to the elastic and inelastic measurements and is planned as continuation proposal of experiment 9-13-829. We aim to close the gap in the different time scales of the dynamics by measuring also NSE on IN15. The expected results might help in the future for pharmaceutical applications and are relevant for colloidal theory.
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BECK Christian; BAEUERLE Famke; CZAKKEL Orsolya; GIRELLI Anita; MATSARSKAIA Olga; PREVOST Sylvain; ROOSEN RUNGE Felix; Frank Schreiber; SEYDEL Tilo and ZHANG Fajun. (2020). Monitoring the short-time diffusion upon approaching the arrested state. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-879
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