This study employs ¹⁹F NMR spectroscopy to demonstrate that BSA induces the time-dependent kinetic unfolding of KH1 proteins, subsequently trapping them in the unfolded state through the formation of intermolecular disulfide bonds. Our findings suggest that the kinetic stability of proteins can be modulated through interactions involving these disulfide bonds.
C. Li, K. Cheng, Q. Wu, X. Liu, Z. Chai, G. Xu, L. Jiang and D. Zhang, Phys. Chem. Chem. Phys., 2026, Accepted Manuscript , DOI: 10.1039/D6CP00245E
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