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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 |
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author | Zhang, Liangliang Sahu, Indra Dev Xu, Man Wang, Yongmei Hu, Xinyu |
author_facet | Zhang, Liangliang Sahu, Indra Dev Xu, Man Wang, Yongmei Hu, Xinyu |
author_sort | Zhang, Liangliang |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5198795 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-51987952017-01-04 Data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding Zhang, Liangliang Sahu, Indra Dev Xu, Man Wang, Yongmei Hu, Xinyu Data Brief Data Article 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. Elsevier 2016-12-21 /pmc/articles/PMC5198795/ /pubmed/28054010 http://dx.doi.org/10.1016/j.dib.2016.12.021 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Data Article Zhang, Liangliang Sahu, Indra Dev Xu, Man Wang, Yongmei Hu, Xinyu Data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding |
title | Data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding |
title_full | Data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding |
title_fullStr | Data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding |
title_full_unstemmed | Data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding |
title_short | Data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding |
title_sort | data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding |
topic | Data Article |
url | 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 |
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