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核糖体失活蛋白(RIPs)属于一类破坏真核细胞糖体的结构、质生物合成毒蛋白,该种蛋白质在生物界广泛存在的,它具有抗肿瘤、抗病毒、抗虫和抗菌等多多样性的生物活性。为了对RIPs功能的探究,相关研究显示,6中I型RIPs具有大量的高度保守结构趋于,并且蛋白内包含了多个丝氨酸(S)、苏氨酸(T)等位点。6种蛋白都为稳定性比较好的蛋白,并且等电点均偏向于碱性,多数蛋白内的亮氨酸(L)含量较高。6种蛋白内都存在信号肽剪切位点,二级结构主要是α螺旋和β折叠。6种蛋白的三维结构都十分的相似,提示了其在功能上是存在相似性的。
Ribosome-inactivating proteins (RIPs) belong to a class of structures that disrupt eukaryotic glycoconjugates. They are proteins that are widely found in the biological world. They are anti-tumor, anti-virus, anti-insect and anti-bacterial Diversity of biological activity. In order to explore the function of RIPs, some researches showed that Type I RIPs in 6 have a large number of highly conserved structures, and the proteins contain multiple serine (S) and threonine (T) sites. All six proteins were stable proteins, and the isoelectric points were all alkaline. Most of the proteins had higher content of leucine (L). There are signal peptide cleavage sites in all six proteins, the secondary structure is mainly α-helix and β-sheet. The three structures of the six proteins are very similar, suggesting that they are functionally similar.