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In this study, certain cysteine residues in Romney sheep wool fibers were labeled more often during stretching tests, particularly under wet conditions, suggesting variability in their disulfide bond contributions to fiber mechanics depending on hydration.

This study provides insight into the specific disulfide bond interactions between keratins and keratin associated proteins, suggesting non-random cysteine interactions crucial for stabilizing hair fiber structure.

Disulfide bonds are crucial for hair structure during keratinization.

This study presents computational modeling and experimental analysis of the HGT protein KAP8.1, identifying key structural features that may influence hair's response to environmental conditions.

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.