TLDR Human and horse hair have similar end groups to wool and feathers.
The study identified the N-terminal and C-terminal residues of human and horse hair keratin, as well as partially reduced hair. The N-terminal groups found were aspartic acid, glutamic acid, glycine, serine, threonine, alanine, and valine, while the C-terminal groups included aspartic acid, glutamic acid, glycine, serine, threonine, and alanine. These findings are consistent with previous research on wool and feather keratin, indicating similar amino acid compositions at the terminal ends of these keratins.
41 citations
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October 2001 in “Experimental Dermatology” The nude gene is important for skin and hair development.
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January 2017 in “Elsevier eBooks” The document concludes that cosmetics need biocompatible, eco-friendly ingredients due to aging populations and demand for effective products.
98 citations
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May 2016 in “Genes” Understanding wool keratin-associated proteins in sheep can help improve wool quality through selective breeding.
62 citations
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October 1999 in “Journal of Investigative Dermatology” New mutations in hair keratin genes can change hair structure and cause monilethrix, with nail issues more common in certain gene mutations.
19 citations
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January 2009 in “International review of cell and molecular biology” Hair's strength and flexibility come from its protein structure and molecular interactions.
