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024 7 _ |a 10.1039/C6SM01837H
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024 7 _ |a 1744-6848
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082 _ _ |a 530
100 1 _ |a Da Vela, Stefano
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245 _ _ |a Kinetics of liquid–liquid phase separation in protein solutions exhibiting LCST phase behavior studied by time-resolved USAXS and VSANS
260 _ _ |a London
|c 2016
|b Royal Soc. of Chemistry
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520 _ _ |a We study the kinetics of the liquid–liquid phase separation (LLPS) and its arrest in protein solutions exhibiting a lower critical solution temperature (LCST) phase behavior using the combination of ultra-small angle X-ray scattering (USAXS) and very-small angle neutron scattering (VSANS). We employ a previously established model system consisting of bovine serum albumin (BSA) solutions with YCl3. We follow the phase transition from sub-second to 104 s upon an off-critical temperature jump. After a temperature jump, the USAXS profiles exhibit a peak that grows in intensity and shifts to lower q values with time. Below 45 °C, the characteristic length scale (ξ) obtained from this scattering peak increases with time with a power of about 1/3 for different sample compositions. This is in good agreement with the theoretical prediction for the intermediate stage of spinodal decomposition where the growth is driven by interface tension. Above 45 °C, ξ follows initially the 1/3 power law growth, then undergoes a significant slowdown, and an arrested state is reached below the denaturation temperature of the protein. This growth kinetics may indicate that the final composition of the protein-rich phase is located close to the high density branch of the LLPS binodal when a kinetically arrested state is reached.
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650 1 7 |a Polymers, Soft Nano Particles and Proteins
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693 _ _ |a Forschungs-Neutronenquelle Heinz Maier-Leibnitz
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700 1 _ |a Braun, Michal K.
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700 1 _ |a Dörr, Andreas
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700 1 _ |a Greco, Alessandro
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700 1 _ |a Möller, Johannes
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700 1 _ |a Fu, Zhendong
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700 1 _ |a Zhang, Fajun
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700 1 _ |a Schreiber, Frank
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773 _ _ |a 10.1039/C6SM01837H
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