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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)...

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Detalles Bibliográficos
Autores principales: Zhang, Liangliang, Sahu, Indra Dev, Xu, Man, Wang, Yongmei, Hu, Xinyu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
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.
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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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