Abstract

The mechanism of interaction of ficin with a graft copolymer of the sodium salt of carboxymethylcellulose and N-vinylimidazole has been investigated by methods of flexible molecular docking, infrared and Raman spectroscopy. Functional groups and fragments of graft copolymer molecules, as well as amino-acid residues forming the primary structure of the enzyme that interacts between the ficin and the graft copolymer, have been identified. It was shown that Raman spectroscopy gives more complete representation of fragments of graft copolymer macromolecules interacting with protein compared to infrared spectroscopy. It has been found that the amino-acid residues forming the active site of ficin were involved in the formation of hydrogen bonds and hydrophobic interactions with the graft copolymer, which led to an increase in the proteolytic activity of the conjugated enzyme.

中文翻译：

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利用分子对接、红外和拉曼光谱研究无花果素与羧甲基纤维素钠盐和N-乙烯基咪唑接枝共聚物的相互作用机制

摘要

无花果素与羧甲基纤维素钠盐与N的接枝共聚物的相互作用机制通过灵活的分子对接、红外和拉曼光谱方法对-乙烯基咪唑进行了研究。已经鉴定出接枝共聚物分子的官能团和片段，以及形成无花果蛋白酶和接枝共聚物之间相互作用的酶的一级结构的氨基酸残基。结果表明，与红外光谱相比，拉曼光谱可以更完整地表征与蛋白质相互作用的接枝共聚物大分子片段。研究发现，形成无花果蛋白酶活性位点的氨基酸残基参与氢键的形成以及与接枝共聚物的疏水相互作用，从而导致缀合酶的蛋白水解活性增加。