Wang, Ying and Lomakin, Aleksey and Ogun, Olutayo and Benedek, George B.
Phase behavior of mixtures of human
lens proteins Gamma D and Beta B1.
Proceedings of the National Academy of Sciences , 107 (30).
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 theoretical analysis of our experimental data, which
enables a quantitative description of our principal experimental
findings. In this way, we have evaluated the magnitude and
temperature dependence of the relevant interprotein interaction
energies. Our findings provide insight into the factors essential
for maintaining lens proteins in a single homogeneous phase,
thereby enabling lens transparency.
||The definitive version of this article is available at PNAS Vol.107 No.3(2010), pp. 13282-13287. www.pnas.org/cgi/doi/10.1073/pnas.1008353107
||cataract; crystallin; phase separation; mixture;
||Science & Engineering > Chemistry
||29 Aug 2012 15:42
|Journal or Publication Title:
||Proceedings of the National Academy of Sciences
||National Academy of Sciences
Repository Staff Only(login required)
||Item control page