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Trichohyalin is a versatile protein involved in hair and skin structure.

Trichohyalin helps in hair and skin cell structure and function by binding calcium and linking proteins.

High glycine–tyrosine keratin-associated proteins help make hair strong and maintain its shape.

Hard α-keratin has a universal molecular structure with a specific superlattice arrangement.

Oxidized trichocyte keratin has a helical dislocation in its structure.

Recombinant keratins can form useful structures for medical applications, overcoming natural keratin limitations.

The Glu413Lys mutation in keratin affects hair stability, while Glu413Asp does not.

Human hair keratin has a 40% α-helix structure that changes to a random coil in 8 M urea.

Disulfide bonds make keratin in hair stronger and tougher.

The study revealed the detailed structure of a keratin dimer, aiding understanding of how intermediate filament proteins function.

Keratin's mechanical properties are influenced by hydrogen bonds and secondary structure, and can be improved with the SPD-2 peptide.

Human hair keratins K85 and K35 create unique filament patterns important for early hair formation.

The study concludes that certain domains in Clostridium histolyticum enzymes are structurally unique, bind calcium to become more stable, and play distinct roles in breaking down collagen, with potential applications in medicine and drug delivery.

Keratin structure in hair is stable at pH 5-6 but disrupts between pH 6-7.

Different conditions affect how hair proteins assemble, and certain mutations can change their structure.

Hair and wool strength is affected by the number and type of bonds in their protein structures, with hair having more protein aggregates than wool.

Trichohyalin in sheep hair follicles may help with structure and calcium binding.

Hair structural proteins are synthesized sequentially in specific cells, offering a new way to study hair proteins and defects.

Different keratin types have unique amino acid patterns that are evolutionarily conserved.

Electrostatic interactions mainly stabilize the binding of peptides to hair keratin.

Cross-linked proteins help maintain the structure of hair, feathers, and hagfish teeth.

Hair proteins have weak spots in their α-helical segments.

Keratin proteins are crucial for hair growth and structure.

PolyQ repeats in neural proteins evolve together, affecting brain function and disease.

Trichohyalin, a protein from pig tongue, was purified and found to have a filamentous structure.