首页    期刊浏览 2024年11月27日 星期三
登录注册

文章基本信息

  • 标题:Phase behavior of mixtures of human lens proteins Gamma D and Beta B1
  • 本地全文:下载
  • 作者:Ying Wang ; Aleksey Lomakin ; Jennifer J. McManus
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2010
  • 卷号:107
  • 期号:30
  • 页码:13282-13287
  • DOI:10.1073/pnas.1008353107
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:We have experimentally determined the coexistence surface characterizing the phase behavior of {gamma}D-{beta}B1-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 {gamma}D and {beta}B1 i.e., large difference of composition in the two coexisting phases. This demixing suggests that the energy of the {gamma}D-{beta}B1 attractive interaction is significantly smaller than the energy of the {gamma}D-{gamma}D attractive interaction. We also observed the lowering of the phase separation temperature upon increasing of the fraction of {beta}B1 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.
  • 关键词:cataract ; crystallin ; phase separation ; mixture
国家哲学社会科学文献中心版权所有