Background: The molecular chaperone function of αB-crystallins is heavily involved in maintaining lens transparency and the development of cataracts.
Objectives: The aim of the study was to investigate whether divalent metal ion binding improves the stability and αB-crystallin chaperone activity.
Methods: In this study, we have developed an H101G αB-crystallin mutant and compared the surface hydrophobicity, chaperone activity, and secondary and tertiary structure with the wild type in the presence and absence of metal ions.