Characterizing the formation of liquid-liquid phase separation by tuning the system by using its lower critical solution temperature
The presence of multivalent salt ions can induce complex phase diagrams in aqueous protein solutions including, with increasing salt concentration, a condensed and a re-entrant dissolution regime. Within the condensed regime, a liquid-liquid phase separation (LLPS) can occur. This LLPS regime may be of fundamental biological and medical interest, because it can play an important role in the self-organization of proteins, both in normal contexts of biological function as well as in pathological pathways. The LLPS regime manifests itself macroscopically by a separation of the originally homogeneous protein solution into microdroplets of a protein-rich phase suspended in the bulk liquid of a protein-poor phase. It is assumed that the LLPS is associated with the formation of protein clusters or aggregates, but the dynamics aspects of the transition are poorly understood. With the frameworks and methods established by our group, we propose a high-resolution backscattering study to access the slow self-diffusive dynamics of protein clusters systematically resolving their nature.
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BECK Christian; BUHL Lena; FEUSTEL Michal; GRIMALDO Marco; MATSARSKAIA Olga; ROOSEN RUNGE Felix; Frank Schreiber; SEYDEL Tilo and ZHANG Fajun. (2017). Characterizing the formation of liquid-liquid phase separation by tuning the system by using its lower critical solution temperature. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-804
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