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[求助]
有誰(shuí)知道精氨酸在蛋白正確折疊組裝時(shí)起到的作用？？？
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如題~很多蛋白的組裝液中都含有精氨酸，有誰(shuí)知道精氨酸在蛋白正確折疊組裝時(shí)起到的作用？？？要分子層面的，是因?yàn)榫彼岬拈L(zhǎng)側(cè)鏈能起到什么緩沖扶持的作用么？我也就是猜測(cè)，請(qǐng)各位大神們幫我解答下啊，不要宏觀的作用，想要分子層面的機(jī)理~~~�。�！謝了！  |
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» 本主題相關(guān)價(jià)值貼推薦，對(duì)您同樣有幫助:
- 帶有精氨酸及尿素的變性蛋白如何純化？
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沒(méi)人么？舉例說(shuō)明也好呀
2樓2013-10-27 23:15:48
3樓2013-10-28 12:08:43
xl_dut
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【答案】應(yīng)助回帖
★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★ ★
感謝參與，應(yīng)助指數(shù) +1
莓林塔(kx444555代發(fā)): 金幣+3, 鼓勵(lì)交流 2013-10-28 15:04:58
莓林塔: 金幣+17, ★★★★★最佳答案, 謝謝 ~ 2013-10-29 17:05:50
感謝參與，應(yīng)助指數(shù) +1
莓林塔(kx444555代發(fā)): 金幣+3, 鼓勵(lì)交流 2013-10-28 15:04:58
莓林塔: 金幣+17, ★★★★★最佳答案, 謝謝 ~ 2013-10-29 17:05:50
|
建議樓主看一下這篇文章！ 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樓2013-10-28 13:14:38
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