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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.

This study found that washing hair after reduction in a permanent waving process allows for significant reformation of disulfide cross-links, enhancing the strength and elasticity of hair fibers.

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.

This study found that treating hair with aqueous KCN converts disulfide bonds to monosulfide crosslinks, affecting the elasticity and crosslink distribution in hair microstructures.