Lomakin A, Asherie N, Benedek G B
Department of Physics, Center for Materials Science and Engineering, and Materials Processing Center, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA.
Proc Natl Acad Sci U S A. 1999 Aug 17;96(17):9465-8. doi: 10.1073/pnas.96.17.9465.
Protein crystallization, aggregation, liquid-liquid phase separation, and self-assembly are important in protein structure determination in the industrial processing of proteins and in the inhibition of protein condensation diseases. To fully describe such phase transformations in globular protein solutions, it is necessary to account for the strong spatial variation of the interactions on the protein surface. One difficulty is that each globular protein has its own unique surface, which is crucial for its biological function. However, the similarities amongst the macroscopic properties of different protein solutions suggest that there may exist a generic model that is capable of describing the nonuniform interactions between globular proteins. In this paper we present such a model, which includes the short-range interactions that vary from place to place on the surface of the protein. We show that this aeolotopic model [from the Greek aiolos ("variable") and topos ("place")] describes the phase diagram of globular proteins and provides insight into protein aggregation and crystallization.
蛋白质结晶、聚集、液-液相分离和自组装在蛋白质结构测定、蛋白质工业加工以及蛋白质凝聚疾病的抑制方面都很重要。为了全面描述球状蛋白质溶液中的此类相变，有必要考虑蛋白质表面相互作用的强烈空间变化。一个困难在于每个球状蛋白质都有其独特的表面，这对其生物学功能至关重要。然而，不同蛋白质溶液宏观性质之间的相似性表明，可能存在一个通用模型，能够描述球状蛋白质之间的非均匀相互作用。在本文中，我们提出了这样一个模型，它包括蛋白质表面不同位置的短程相互作用。我们表明，这个风域模型（源自希腊语“aiolos”（“可变的”）和“topos”（“位置”））描述了球状蛋白质的相图，并为蛋白质聚集和结晶提供了见解。
