Structural basis of eye lens transparency: light scattering by concentrated solutions of bovine alpha-crystallin proteins.
Structural basis of eye lens transparency: light scattering by concentrated solutions of bovine alpha-crystallin proteins.
复制标题
眼睛晶状体透明度的结构基础：牛α-晶状体蛋白浓缩溶液的光散射。
DOI：
10.1016/s0006-3495(96)79477-8
复制
发表时间：
1996
影响因子：
3.4
通讯作者：
J. Clauwaert
中科院分区：
文献类型：
--
作者：
J. Xia;Qinghua Wang;S. Tatarkova;T. Aerts;J. Clauwaert
晶体蛋白的短程有序性确实解释了眼睛透镜的透明度。为了定量地解释这种高浓度蛋白质溶液的溶液结构，必须知道蛋白质的流体动力学结构和颗粒间相互作用。为此，研究了α-晶状体蛋白浓溶液的光散射。从α-晶状体蛋白在稀释溶液中的溶液参数的详细知识开始，使用光散射研究了高达360 mg/ml的浓缩溶液的结构。我们的研究结果表明，在大分子结构的细微变化，如光学各向异性或结构不对称的一部分的α-晶体蛋白，这会导致溶质光散射的异质性，可以显着增加光散射的α-晶体蛋白，并导致溶液不透明。
Short range order of the crystallins does account for the transparency of the eye lens. To explain the solution structure of this highly concentrated protein solution on a quantitative basis, the hydrodynamic structure and the interparticle interactions of the proteins have to be known. For that purpose, the light scattering of concentrated solutions of alpha-crystallin has been studied. Starting from the detailed knowledge of the solution parameters of alpha-crystallin in diluted solutions, the structure of concentrated solutions up to 360 mg/ml has been studied using light scattering. Our results indicate that subtle changes in the macromolecular structure such as optical anisotropy or structural asymmetry for part of the alpha-crystallins, which results in solute light-scattering heterogeneity, can dramatically increase the light scattering by the alpha-crystallins and cause solution opacity.