STRUCTURES OF TERMINASE SUBUNITS OF BACTERIOPHAGE T4: VIRUS ASSEMBLY

噬菌体P22 Proapsids含有一个内部支架 离开结构的蛋白质。当DNA被包装进。 被膜蛋白外壳。支架蛋白与细胞共同组装 外壳蛋白。大约200个支架蛋白分子 与大约400个分子的外壳蛋白组装形成 普罗卡西德。对支架蛋白的研究表明，C-末端 FIFF有能力与涂层正确地结合在一起。凝胶 研究表明，较短的脚手架的副本更多 这些前衣壳中的蛋白质。用STEM进行质量测量发现 Proapsids与半长支架蛋白组装在一起 含有大约两倍数量的支架分子。这 表明弹壳填充机构可能在 普罗卡西德组合物。蛋白骨架蛋白形成的蛋白原 为了测试罐头，人们正在测量各种长度。大约是 对于由全、半和三部分组成的衣壳，得到相同的质量 三分之一长度的支架蛋白。

Bacteriophage P22 procapsids contain an internal scaffolding protein which leaves the structure.when the DNA is packaged into the. coat protein shell. The scaffolding protein co-assembles with the coat protein. Approximately 200 molecules of scaffolding protein assemble with about 400 molecules of coat protein to form the procapsid. Studies of the scaffolding protein showed that C-terminal fiagments are competent to co-assemble with the coat properly. Gel studies suggested that there were more copies of shorter scaffolding proteins in these procapsids. Mass measurements with the STEM found that procapsids assembled with half-length scaffolding protein contained about twice the number of scaffolding molecules. This suggests that a shell-filling mechanism may be operating during procapsid assembly. Procapsids formed with scaffolding proteins of various lengths are being measured to test tins. Approximately the same masses are obtained for capsids assembled with full, half, and one third length scaffolding protein.