Bacteriorhodopsin (BR ) 展出,作为在象功能的信息材料的 Halobacterium salinarum,唯一的 photoresponsive 行为,和表演诺言的膜蛋白质。有缬氨酸(BR-D96V ) 代替的第 96 丁氨二酸酸的 BR 的新异种被获得然后在一个合成聚合物矩阵的 BR-D96V 的一部合成电影在这研究被准备。变异的 BR-D96V 在 bacterio 视蛋白被表示由基因工程的缺乏的 halobacterial 紧张(L33 ) 。尽管缬氨酸是很恐水病的,也就是,这点异种保留基本生物活动光电并且对光反应变色回答。不过,在 BR 异种中间的 M 的一生比在中立水的答案的野类型的 BR 的长将近二个数量级,它作为信息材料有益于它的潜在的应用程序。M 一生进一步显著地在把 BR-D96V 嵌进以后被延长 poly (乙烯基白酒)(PVA ) 。BR-D96V 是很敏感的与野类型的 BR 和另一 BR 异种比较浇内容,这也被发现。
Bacteriorhodopsin (BR) exhibits, as a membrane protein in Halobacterium salinarum, unique photoresponsive behaviors, and shows promise as a functional information material. A new mutant of BR with the 96th aspartic acid replaced by valine (BR-D96V) was obtained and then a composite film of BR-D96V in a synthetic polymer matrix was prepared in this research. The mutant BR-D96V was expressed in a bacterio-opsin deficient halobacterial strain (L33) by gene engineering. Although valine is very hydrophobic, this point mutant keeps the basic biological activities, namely, photoelectric and photochromic responses. Nevertheless, the lifetime of M intermediate in the BR mutant is nearly two orders of magnitude longer than that of wild-type BR in neutral aqueous solution, which benefits its potential application as an information material. The M lifetime is further signifi- cantly prolonged after embedding BR-D96V into poly(vinyl alcohol) (PVA). It was also found that BR-D96V is very sensitive to water content in comparison with wild-type BR and another BR mutant.