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Data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding
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) [1]. Data was obtained by circular dichroism (CD) spectroscopy to investigate potential β-lactoglobulin (β-Lg)...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5198795/ https://www.ncbi.nlm.nih.gov/pubmed/28054010 http://dx.doi.org/10.1016/j.dib.2016.12.021 |
Sumario: | 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) [1]. 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. |
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