Suppr超能文献

(-)-表没食子儿茶素没食子酸酯与金属离子结合后β-乳球蛋白构象分析的数据。

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

作者信息

Zhang Liangliang, Sahu Indra Dev, Xu Man, Wang Yongmei, Hu Xinyu

机构信息

Key Lab. of Biomass Energy and Material, Jiangsu Province; Institute of Chemical Industry of Forest Products, CAF, Nanjing 210042, China.

Chemistry and Biochemistry Department, Miami University, Oxford, OH 45056, USA.

出版信息

Data Brief. 2016 Dec 21;10:474-477. doi: 10.1016/j.dib.2016.12.021. eCollection 2017 Feb.

Abstract

This data article contains complementary results related to the paper "Effect of metal ions on the binding reaction of (-)-epigallocatechin gallate to -lactoglobulin" (Zhang et al., 2017) [1]. Data was obtained by circular dichroism (CD) spectroscopy to investigate potential -lactoglobulin (-Lg) conformational changes with different concentrations of EGCg and Cu or Al added to -Lg. 500 µL of the 25 µM -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 -Lg-Cu, -Lg-Al and -Lg-EGCg interaction resulted in unfolding of the secondary structure of -Lg.

摘要

本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》(Zhang等人,2017年)[1]相关的补充结果。通过圆二色光谱(CD)获得数据,以研究在向β-乳球蛋白(β-Lg)中添加不同浓度的表没食子儿茶素没食子酸酯(EGCg)和铜或铝时,β-乳球蛋白(β-Lg)潜在的构象变化。测量了500微升含有EGCg(25微摩尔)或金属离子(0 - 500微摩尔)的25微摩尔β-Lg溶液,并记录光谱。本文中呈现的CD光谱数据表明,β-Lg-铜、β-Lg-铝和β-Lg-EGCg相互作用导致β-Lg二级结构展开。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ac6/5198795/d01bf69982a3/mmc1.jpg

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验