Experimental data on pH-dependent structural interactions between plant proteins and red cabbage polyphenols

Published: 25 August 2026| Version 1 | DOI: 10.17632/frzc9g88rj.1
Contributor:
Marcin Kurek

Description

This dataset contains experimental data supporting the study “Molecular Interplay Between Plant Proteins and Polyphenols: pH as a Switch for Structural and Functional Assembly”. The study investigated pH-dependent interactions between red cabbage polyphenols and three underutilized plant protein sources: mustard protein concentrate, evening primrose protein, and sunflower meal protein isolate. The deposited data include intrinsic fluorescence spectroscopy measurements and free sulfhydryl group determinations obtained for protein and protein–polyphenol systems under different pH conditions. Fluorescence data provide information on changes in the microenvironment of aromatic amino acid residues and protein conformation, while sulfhydryl group measurements provide complementary information on conformational changes and thiol accessibility. Together, these datasets support structural characterization of pH-dependent protein–polyphenol interactions and contribute to understanding the relationship between molecular assembly and the functional behavior of plant protein systems.

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