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 -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.

Effect of metal ions on the binding reaction of (-)-epigallocatechin gallate to β-lactoglobulin.

The effects of metal ions (Cu, Sn, Zn, Mn, Al and Fe) on the interaction between (-)-epigallocatechin-3-gallate (EGCg) and β-lactoglobulin (β-Lg) were investigated via fluorescence and circular dichroism (CD) spectroscopy. The results of the fluorescence titration experiment demonstrated that the addition of Cu increases the quenching efficiency of EGCg to β-Lg by more than EGCg alone, while Mn, Al and Zn decrease the quenching efficiency of EGCg to β-Lg by less than EGCg alone. [β-Lg-Mn], [β-Lg-Al], [β-Lg-Zn] and [β-Lg-Sn] obviously decreased the apparent binding affinities (K) of EGCg to β-Lg by 95.

Magnetic Resonance Spectra and Statistical Geometry.

Methods of statistical geometry are introduced which allow one to estimate, on the basis of computable criteria, the conditions under which maximally informative data may be collected. We note the important role of constraints which introduce curvature into parameter space and discuss the appropriate mathematical tools for treating curvature effects. Channel capacity, a term from communication theory, is suggested as a useful figure of merit for estimating the information content of spectra in the presence of noise.