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蛋白质从新生态到天然态的折叠中 ,大多数都依赖于已经存在的功能蛋白质即蛋白质分子伴侣。在目前研究的 2 0多种分子伴侣中 ,对于Hsp6 0如E .coli中的GroEL和GroES的功能和结构研究得最多 ,也最详细 ,其主要功能是帮助非天然态的多肽折叠成具有生物活性的天然态功能蛋白质。蛋白质分子伴侣除折叠功能外 ,还可以作为药物如格尔德霉素 (geldanamycin ,GA)作用的靶点 ,GA通过与蛋白质分子伴侣Hsp90作用 ,影响其底物的正确折叠而被降解 ,达到其作用之目的。
Most of the folding of the protein from the new ecosystem to the natural state depends on the already existing functional protein, the protein chaperone. Of the 20 molecular chaperones currently studied, the function and structure of GroEL and GroES in Hsp60 such as E. coli are the most studied and most detailed, and their main function is to help the non-natural polypeptide be folded into a living organism Active natural state functional protein. In addition to its folding function, the protein chaperone can also serve as a target for the action of drugs such as geldanamycin (GA), which is degraded by interacting with the protein chaperone Hsp90 and affecting the correct folding of the substrate Purpose of the role.