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[求助]
有谁知道精氨酸在蛋白正确折叠组装时起到的作用？？？
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如题~很多蛋白的组装液中都含有精氨酸，有谁知道精氨酸在蛋白正确折叠组装时起到的作用？？？要分子层面的，是因为精氨酸的长侧链能起到什么缓冲扶持的作用么？我也就是猜测，请各位大神们帮我解答下啊，不要宏观的作用，想要分子层面的机理~~~！！！谢了！  |
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- 带有精氨酸及尿素的变性蛋白如何纯化？
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没人么？举例说明也好呀
2楼2013-10-27 23:15:48
3楼2013-10-28 12:08:43
xl_dut
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莓林塔(kx444555代发): 金币+3, 鼓励交流 2013-10-28 15:04:58
莓林塔: 金币+17, ★★★★★最佳答案, 谢谢 ~ 2013-10-29 17:05:50
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莓林塔: 金币+17, ★★★★★最佳答案, 谢谢 ~ 2013-10-29 17:05:50
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建议楼主看一下这篇文章！ Biotechnol Prog. 2004 Sep-Oct;20(5):1301-8. Role of arginine in protein refolding, solubilization, and purification. Tsumoto K, Umetsu M, Kumagai I, Ejima D, Philo JS, Arakawa T. Source Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba-ku, Sendai 980-8579, Japan. tsumoto@mail.tains.tohoku.ac.jp Abstract Recombinant proteins are often expressed in the form of insoluble inclusion bodies in bacteria. To facilitate refolding of recombinant proteins obtained from inclusion bodies, 0.1 to 1 M arginine is customarily included in solvents used for refolding the proteins by dialysis or dilution. In addition, arginine at higher concentrations, e.g., 0.5-2 M, can be used to extract active, folded proteins from insoluble pellets obtained after lysing Escherichia coli cells. Moreover, arginine increases the yield of proteins secreted to the periplasm, enhances elution of antibodies from Protein-A columns, and stabilizes proteins during storage. All these arginine effects are apparently due to suppression of protein aggregation. Little is known, however, about the mechanism. Various effects of solvent additives on proteins have been attributed to their preferential interaction with the protein, effects on surface tension, or effects on amino acid solubility. The suppression of protein aggregation by arginine cannot be readily explained by either surface tension effects or preferential interactions. In this review we show that interactions between the guanidinium group of arginine and tryptophan side chains may be responsible for suppression of protein aggregation by arginine. |
4楼2013-10-28 13:14:38
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