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This study suggests that increased amounts of less stable disulfide conformers in hair shafts may be linked to the brittleness observed in trichothiodystrophy.

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 found that xylanase and pectinase enzymes clean wool and specialty hair fibers as effectively as soap, without causing physical damage, whereas resinase was not effective.

This study suggests that the cell membrane complex in hair cuticles contains hydrophilic regions with disulfide bonds allowing polymer uptake and hydrophobic lamella-like lipid layers.

This study investigated multiple alkaline oxidative dehairing systems and found a consistent reaction mechanism for disulfide cleavage across systems, enhancing hair solubilization by enabling structural swelling and water uptake.