Casein as a model intrinsically disordered protein: Impact of salt on the internal diffusive dynamics in solution
We aim to investigate fundamental properties of intrinsically disordered proteins (IDPs) in aqueous solution from a polymer physics perspective as part of a collaborative project jointly funded by the French ANR and German DFG agencies and involving both experimental and theory groups. Caseins represent a model system for IDPs that is abundant, safe, non-toxic, well soluble, commercially available, and technologically relevant. Here, we specifically aim to investigate the influence of calcium Ca2+ ions on the internal diffusive dynamics of ß-casein in aqueous solution. This systematic dependence on the Ca2+ concentration constitutes a clearly missing important piece of information for the physiologically relevant aqueous solution setting of casein micelles. This study will prepare the ground for future studies of the phase behavior of casein in aqueous solution, addressing their association and assembly, involving processes linked to liquid-liquid phase separation. We will use BATS that has proven to be ideally suited to access the internal diffusive dynamics of proteins in solution. This work will be part of a future PhD project (student appointed, but not yet arrived).
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SEYDEL Tilo; BECK Christian; CHAKRABORTY Saikat; GRUNDEL Anna; MATEO MINARRO Laura; MOROZOVA Tatiana; MOSCA Ilaria; NASRO Roody; ROOSEN RUNGE Felix and Frank Schreiber. (2023). Casein as a model intrinsically disordered protein: Impact of salt on the internal diffusive dynamics in solution. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-1046
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