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Spinodal surface of a free energy model for eyelens protein mixtures: Relevance for cataracts

机译:眼睑蛋白质混合物的自由能模型的微晶表面:对白内障的相关性

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We studied the phase behavior of a model binary mixture of eye lens crystallin proteinsusing first-order thermodynamic perturbation theory. The instability boundary, or spinodal surface,was found to be very sensitive to the strength of the attraction between the two proteins, and also torespond to this interprotein attraction strength in a non-monotonic fashion. In particular, in the caseof either weak or strong attractions, these eye lens solutions become thermodynamically unstable.Interestingly, attraction strengths that correspond closely to those of proteins isolated from the livinglens fall right within the stable region of the phase diagram. This non-monotonic stability suggestsnew molecular mechanisms for eye lens opacification in cataract.
机译:我们研究了眼睛晶状体蛋白质蛋白质蛋白质一阶热力学扰动理论的模型二元混合物的相行为。发现不稳定的边界或旋趾表面对两种蛋白质之间的吸引力非常敏感,并且还以非单调的方式诠释其诠释蛋白引起的引起。特别是,在弱者或强烈的景点中,这些眼镜溶液变得热力学不稳定。互相兴趣的吸引强度,其对应于从LINESLENS中分离的蛋白质的吸引力落入相图的稳定区域内。这种非单调的稳定性表明了白内障眼晶透镜渗透的分子机制。

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