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Photon correlation spectroscopy and light scattering of eye lens proteins at high concentrations.

机译:光子相关光谱法和高浓度眼镜片蛋白质的光散射。

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摘要

The bovine eye lens protein, alpha L crystallin, has been studied with photon correlation spectroscopy and statical light scattering in the concentration range up to 200 g/l in different solvent conditions. At higher concentration (c greater than 70 g/l) the scattering behavior is quite complicated, which results in nonexponential correlation functions. Three methods have been used for the analysis of these correlation functions, namely, cumulant analysis, sum of two exponentials analysis, and exponential sampling method. These methods resulted in very similar results. The highly concentrated solutions contain two scattering entities: the single alpha L crystallin and a rather heterogeneous population of large clusters. The statical light-scattering experiments can be interpreted in the same way and gave consistent results for the dimensions of the large scattering units. The formation of these clusters, which are strong light scatterers, is superimposed on an increasing degree of correlation between the bulk of the alpha L-crystallins, resulting in a net decrease of light scattering as a function of concentration.
机译:牛眼晶状体蛋白,αL晶状体蛋白,已通过光子相关光谱法和在不同溶剂条件下浓度范围高达200 g / l的静态光散射进行了研究。在较高浓度(c大于70 g / l)下,散射行为非常复杂,这导致了非指数相关函数。已使用三种方法来分析这些相关函数,即累积量分析,两个指数分析之和和指数采样法。这些方法产生了非常相似的结果。高度浓缩的溶液包含两个散射实体:单个αL晶状蛋白和相当异质的大簇簇。静态光散射实验可以用相同的方式解释,并且对于大散射单元的尺寸给出一致的结果。这些簇是强光散射体,其形成与大量αL-晶状体蛋白之间相关性的增加重叠,导致光散射随浓度的变化而净减少。

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