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This study proposed a network model for the cross-linked structure of keratin-associated proteins in hair and wool fibers, suggesting notable differences between the two, potentially affecting hair fiber elasticity.

In this study, treating hair with thioglycolic acid was found to alter disulfide bond patterns in keratin-associated proteins, shifting them from an ellipsoidal to a near-spherical shape.

In this study, researchers mapped cysteine accessibility in wool keratins and KAPs, revealing that certain cysteines in keratin end domains and Types I and II rod domains are accessible and likely involved in forming disulfide bonds.

This study observed that repeated perm treatments decrease disulfide bonds in hair due to their conversion largely into cysteic acid, affecting the waving efficiency depending on the reduction agent used.

In this study, treatment with aqueous KCN selectively converted disulfide bonds to monosulfide crosslinks in hair, leading to changes in microstructural properties and rubberlike elasticity under specific laboratory conditions.