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

AI Article Synopsis

  • This data article complements the research paper on how metal ions affect the binding of (-)-epigallocatechin gallate (EGCg) to beta-lactoglobulin (-Lg).
  • The study used circular dichroism (CD) spectroscopy to assess changes in the structure of -Lg with varying levels of EGCg and metal ions (Cu and Al).
  • Results showed that the interactions of -Lg with Cu, Al, and EGCg led to the unfolding of -Lg's secondary structure.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5198795PMC
http://dx.doi.org/10.1016/j.dib.2016.12.021DOI Listing

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