Temperature driven structural changes of a protein-rich phase after liquid-liquid phase separation
Effective interactions of proteins in aqueous solution play a crucial role in understanding protein crystallization and many physiological diseases related to protein association [1]. Experimental results on the phase behavior of protein solutions show a variety of phenomena including metastable liquid-liquid phase separation (LLPS) [2], arrested spinodal decomposition [3], transient clusters [4, 5] and reentrant condensation in the presence of multivalent counterions [6-8]. The metastable LLPS is related to a short-ranged isotropic attraction or attractive patches; the physical mechanism behind the attraction, however, still remains unclear. Depending on the attractive mechanism and volume fraction, the protein-rich phase can be in a liquid or an arrested state, leading to gelation [9].
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WOLF Marcell; JACOBS Robert; ROOSEN RUNGE Felix; SAUTER Andrea; Frank Schreiber; SCHWEINS Ralf; SKODA Maximilian and ZHANG Fajun. (2013). Temperature driven structural changes of a protein-rich phase after liquid-liquid phase separation. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-507
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