Measurement of biomolecular interactions and association via light scattering

1. 在总蛋白浓度高达35 g/l的条件下，在核糖核酸酶带净正电荷，其他蛋白质带净负电荷的条件下，在不同的组成和pH值下，测量了卵清蛋白、核糖核酸酶A和卵样蛋白三种蛋白质以及三种蛋白质的二元混合物的光散射浓度依赖性。在三个模型的背景下解释了浓度依赖性：一个统计热力学模型和有效硬粒子模型的两个扩展，以允许二元混合物中物种之间存在非加性相互作用（D. Wu, a . Minton）。

1. The concentration dependence of light scattering of three proteins, ovalbumin, ribonuclease A, and ovomucoid, and binary mixtures of the three proteins were measured at various compositions and pH values at total protein concentrations of up to 35 g/l, under conditions such that ribonuclease bears a net positive charge and the other proteins bear a net negative charge. The concentration dependence was interpreted in the context of three models: a statistical thermodynamic model and two extensions of the effective hard particle model generalized to allow for the presence of non-additive interactions between species in a binary mixture (D. Wu, A. Minton). 2. Experiments were performed to determine whether quantitative composition gradient light scattering experiments can be performed using a fluorescence spectrophotometer in place of a dedicated light scattering photometer. Results obtained so far are encouraging, but further work will be required in order to achieve the requisite reproducibility.