Structure of arrested protein gel in the presence of a trivalent salt
We propose to investigate the structure of arrested protein gel which is formed via an arrested spinodal decomposition in protein-salt solutions upon liquid-liquid phase separation (LLPS). We use our model systems of bovine and human serum albumin (BSA/HSA) with YCl3 which show LLPS and a lower critical solution temperature (LCST) phase behavior. By a temperature jump, the protein-salt solutions with a high volume fraction (larger than 10%) undergoes an arrested spinodal decomposition. Using SANS we aim to cover the relevant length scale from the local structure to the bicontinuous network. In particularly, we are interested in characterizing the interface between the dilute phase and the glassy-like dense phases as well as the local structure of the glassy-like dense phases.
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ZHANG Fajun; DA VELA Stefano; FEUSTEL Michal; GRILLO Isabelle; GRIMALDO Marco; JACOBS Robert; SAUTER Andrea; Frank Schreiber; SCHWEINS Ralf and SEYDEL Tilo. (2014). Structure of arrested protein gel in the presence of a trivalent salt. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-565
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