A model of attractive interactions to account for fluid-fluid phase separation of protein solutions
A model of attractive interactions to account for fluid-fluid phase separation of protein solutions
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DOI：
10.1063/1.471843
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发表时间：
1996-08-22
影响因子：
4.4
通讯作者：
Tardieu, A
中科院分区：
文献类型：
--
作者：
Malfois, M;Bonnete, F;Tardieu, A
据报道，浓缩的伽马晶体蛋白和溶菌酶溶液在冷却到临界温度以下时会发生液-液相分离。这一行为受控于溶液中大分子间的弱作用力。我们在法国奥赛的同步辐射设施Lure上使用了小角x射线散射来分析相互作用势。一个依赖于三个参数的吸引相互作用模型，即蛋白质直径、势深度和射程，能够解释高温下测量的X射线结构因子和低温相分离。虽然范德华作用力可能是吸引人的相互作用势的起源，但其他更具体的效应也对蛋白质相图有贡献。(C)1996年美国物理研究所。
Concentrated gamma-crystallin and lysozyme solutions have been reported to undergo a fluid-fluid phase separation when cooled below a critical temperature. This behavior is under control of the weak forces acting in solution between macromolecules. We have used small angle x-ray scattering at the synchrotron radiation facility LURE (Orsay, France) to analyze the interaction potentials. A model of attractive interactions which depends upon three parameters, protein diameter, potential depth, and range, is able to account for both the x-ray structure factors measured at high temperature and for the low temperature phase separation. Although van der Waals forces could be at the origin of the attractive interaction potentials, other more specific effects also contribute to the protein phase diagrams. (C) 1996 American Institute of Physics.