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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 review discusses the complexities and uncertainties in the pathways and mechanisms for disulfide bond formation in multicellular organisms and reports no new experimental findings.

Disulfide bonds are crucial for hair structure during keratinization.

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