We have experimentally determined the coexistence surface characterizing the phase behavior of γD-βB1-water ternary solutions. The coexistence surface fully describes the solution conditions, i.e., temperature, protein concentration, and protein composition, at which liquid-liquid phase separation occurs in a ternary solution. We have observed a significant demixing of γD and βB1 i.e., large difference of composition in the two coexisting phases. This demixing suggests that the energy of the γD-βB1 attractive interaction is significantly smaller than the energy of the γD-γD attractive interaction. We also observed the lowering of the phase separation temperature upon increasing of the fraction of βB1 in solution. We provide a the...
Self-assembly is central to the formation of biological structures and has generated a number of syn...
The P23T mutant of human γD-crystallin (HGD) is associated with cataract. We have previously investi...
β-Crystallins are structural proteins maintaining eye lens transparency and opacification. Previous ...
We have experimentally determined the coexistence surface characterizing the phase behavior of γD-β...
Liquid-liquid phase separation occurs in young mammalian eye lenses and in concentrated solutions of...
We model light-scattering cross sections of concentrated aqueous mixtures of the bovine eye lens pro...
We present measurements of the phase-separation temperature (Tph(4,a)) as a function of overall prot...
Investigating proteins with techniques such as NMR or neutron scattering frequently requires the par...
Liquid–liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
We report our use of static and dynamic light scattering techniques to study aqueous solutions of th...
We report the magnetic field dependence of 1/T1 of solvent water protons and deuterons (nuclear magn...
Liquid–liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
Liquid-liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
AbstractHuman lens β-crystallin contains four acidic (βA1→βA4) and three basic (βB1→βB3) subunits. T...
Cataract, the leading cause of blindness worldwide, has motivated a variety of investigations into t...
Self-assembly is central to the formation of biological structures and has generated a number of syn...
The P23T mutant of human γD-crystallin (HGD) is associated with cataract. We have previously investi...
β-Crystallins are structural proteins maintaining eye lens transparency and opacification. Previous ...
We have experimentally determined the coexistence surface characterizing the phase behavior of γD-β...
Liquid-liquid phase separation occurs in young mammalian eye lenses and in concentrated solutions of...
We model light-scattering cross sections of concentrated aqueous mixtures of the bovine eye lens pro...
We present measurements of the phase-separation temperature (Tph(4,a)) as a function of overall prot...
Investigating proteins with techniques such as NMR or neutron scattering frequently requires the par...
Liquid–liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
We report our use of static and dynamic light scattering techniques to study aqueous solutions of th...
We report the magnetic field dependence of 1/T1 of solvent water protons and deuterons (nuclear magn...
Liquid–liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
Liquid-liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
AbstractHuman lens β-crystallin contains four acidic (βA1→βA4) and three basic (βB1→βB3) subunits. T...
Cataract, the leading cause of blindness worldwide, has motivated a variety of investigations into t...
Self-assembly is central to the formation of biological structures and has generated a number of syn...
The P23T mutant of human γD-crystallin (HGD) is associated with cataract. We have previously investi...
β-Crystallins are structural proteins maintaining eye lens transparency and opacification. Previous ...