Driedonks R A, Krijgsman P C, Mellema J E
Philos Trans R Soc Lond B Biol Sci. 1976 Nov 30;276(943):131-41. doi: 10.1098/rstb.1976.0104.
The states of aggregation of alfalfa mosaic virus (AMV) protein have been characterized by sedimentation velocity experiments and electron microscopy. The main association product is a spherical particle with an s value of about 30S. It is highly likely that the assembly of this particle starts with dimers of the 25000 molecular mass unit resulting in an icosahedral particle made of 30 dimers. No intermediate aggregation products have been detected. The clustering pattern of the protein in the cylindrical part of the AMV capsid favours the concept of dimers as the active assembling units.
通过沉降速度实验和电子显微镜对苜蓿花叶病毒(AMV)蛋白的聚集状态进行了表征。主要的缔合产物是一种沉降系数约为30S的球形颗粒。这种颗粒的组装很可能始于分子量为25000道尔顿的二聚体,形成由30个二聚体组成的二十面体颗粒。未检测到中间聚集产物。AMV衣壳圆柱形部分中蛋白质的聚集模式支持二聚体作为活性组装单元的概念。