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Data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding

机译:(-)-表没食子儿茶素没食子酸酯和金属离子结合后的β-乳球蛋白构象分析数据

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This data article contains complementary results related to the paper “Effect of metal ions on the binding reaction of (-)-epigallocatechin gallate to β -lactoglobulin” (Zhang et al., 2017) . Data was obtained by circular dichroism (CD) spectroscopy to investigate potential β -lactoglobulin ( β -Lg) conformational changes with different concentrations of EGCg and Cu 2+ or Al 3+ added to β -Lg. 500 μL of the 25 μM β -Lg solution containing EGCg (25 μM) or metal ions (0–500 μM) were measured, and the spectra were recorded. CD spectroscopy data present in this article indicated that the β -Lg-Cu, β -Lg-Al and β -Lg-EGCg interaction resulted in unfolding of the secondary structure of β -Lg.
机译:该数据文章包含与论文“金属离子对(-)-表没食子儿茶素没食子酸酯与β-乳球蛋白结合反应的影响”有关的补充结果(Zhang等人,2017)。通过圆二色性(CD)光谱获得数据,以研究在β-Lg中添加不同浓度的EGCg和Cu 2+或Al 3+时潜在的β-乳球蛋白(β-Lg)构象变化。测量了500μL的25μM含EGCg(25μM)或金属离子(0–500μM)的β-Lg溶液,并记录了光谱。本文中的CD光谱数据表明,β-Lg-Cu,β-Lg-Al和β-Lg-EGCg相互作用导致β-Lg二级结构的展开。

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